Understanding the interplay between CpG island-associated gene promoters and H3K4 methylation
Open accessAbstract
The precise regulation of gene transcription is required to establish and maintain cell type-specific gene expression programs during multicellular development. In addition to transcription factors, chromatin, and its chemical modification, play a central role in regulating gene expression. In vertebrates, DNA is pervasively methylated at CG dinucleotides, a modification that is repressive to transcription. However, approximately 70% of vertebrate gene promoters are associated with DNA elements called CpG islands (CGIs) that are refractory to DNA methylation. CGIs integrate the activity of a range of chromatin-regulating factors that can post-translationally modify histones and modulate gene expression. This is exemplified by the trimethylation of histone H3 at lysine 4 (H3K4me3), which is enriched at CGI-associated gene promoters and correlates with transcriptional activity. Through studying H3K4me3 at CGIs it has become clear that CGIs shape the distribution of H3K4me3 and, in turn, H3K4me3 influences the chromatin landscape at CGIs. Here we will discuss our understanding of the emerging relationship between CGIs, H3K4me3, and gene expression.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
CpGs in CG-poor regions are generally methylated, while CpGs within CGIs remain unmethylated in normal cells and aberrantly hypermethylated in cancer.
“The CpGs in CG-poor regions are generally methylated, while CpGs within CGIs remain unmethylated in normal cells49 and aberrantly hypermethylated in cancer2,50.”
From Alternative promoters in CpG depleted regions are prevalently associated with epigenetic misregulation of liver cancer transcriptomes (2023) · cites this paper as [49]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Heintzman, N. D., Stuart, R. K., Hon, G., Fu, Y., Ching, C. W., Hawkins, R. D., Barrera, L. O., Van Calcar, S., Qu, C., Ching, K. A., et al. (2007) · Nature Genetics · doi:10.1038/ng1966 · Cited by 3,398 · see citing works
Genome-scale DNA methylation maps of pluripotent and differentiated cells
Meissner, A., Mikkelsen, T. S., Gu, H., Wernig, M., Hanna, J., Sivachenko, A., Zhang, X., Bernstein, B. E., Nusbaum, C., Jaffe, D. B., et al. (2008) · Nature · doi:10.1038/nature07107 · Cited by 2,536 · see citing works
Histone modifications at human enhancers reflect global cell-type-specific gene expression
Heintzman, N. D., Hon, G. C., Hawkins, R. D., Kheradpour, P., Stark, A., Harp, L. F., Ye, Z., Lee, L. K., Stuart, R. K., Ching, C. W., et al. (2009) · Nature · doi:10.1038/nature07829 · Cited by 2,533 · see citing works
Genome-wide mapping of HATs and HDACs reveals distinct functions in active and inactive genes
Wang, Z., Zang, C., Cui, K., Schones, D. E., Barski, A., Peng, W., & Zhao, K. (2009) · Cell · doi:10.1016/j.cell.2009.06.049 · Cited by 1,344 · see citing works
JmjC-domain-containing proteins and histone demethylation
Klose, R. J., Kallin, E. M., & Zhang, Y. (2006) · Nature Reviews Genetics · doi:10.1038/nrg1945 · Cited by 1,290 · see citing works
Self-citationH3K4me3 breadth is linked to cell identity and transcriptional consistency
Benayoun, B. A., Pollina, E. A., Ucar, D., Mahmoudi, S., Karra, K., Wong, E. D., Devarajan, K., Daugherty, A. C., Kundaje, A. B., Mancini, E., et al. (2014) · Cell · doi:10.1016/j.cell.2014.06.027 · Cited by 536 · see citing works
Understanding nucleosome dynamics and their links to gene expression and DNA replication
Lai, W. K. M., & Pugh, B. F. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.47 · Cited by 495 · see citing works
Horton, J. R., Upadhyay, A. K., Qi, H. H., Zhang, X., Shi, Y., & Cheng, X. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1753 · Cited by 389 · see citing works
Structural Biology of Human H3K9 Methyltransferases
Wu, H., Min, J., Lunin, V. V., Antoshenko, T., Dombrovski, L., Zeng, H., Allali-Hassani, A., Campagna-Slater, V., Vedadi, M., Arrowsmith, C. H., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0008570 · Cited by 268 · see citing works
In vivo targeting of de novo DNA methylation by histone modifications in yeast and mouse
Morselli, M., Pastor, W. A., Montanini, B., Nee, K., Ferrari, R., Fu, K., Bonora, G., Rubbi, L., Clark, A. T., Ottonello, S., et al. (2015) · eLife · doi:10.7554/elife.06205 · Cited by 167 · see citing works
Paf1C regulates RNA polymerase II progression by modulating elongation rate
Hou, L., Wang, Y., Liu, Y., Zhang, N., Shamovsky, I., Nudler, E., Tian, B., & Dynlacht, B. D. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1904324116 · Cited by 129 · see citing works
Flagged first, then by citations
Research works printed but not linked: 256
- [1]Lorch Y. LaPointe J.W. Kornberg R.D. Nucleosomes inhibit the initiation of transcription but allow chain elongation with the displacement of histones Cell 49 1987 203 210 10.1016/0092-8674(87)90561-7 3568125 · DOI
- [2]Li B. Carey M. Workman J.L. The role of chromatin during transcription Cell 128 2007 707 719 10.1016/j.cell.2007.01.015 17320508 · DOI
- [3]Levine M. Cattoglio C. Tjian R. Looping back to leap forward: transcription enters a new era Cell 157 2014 13 25 10.1016/j.cell.2014.02.009 24679523 PMC4059561 · DOI
- [4]Venkatesh S. Workman J.L. Histone exchange, chromatin structure and the regulation of transcription Nat. Rev. Mol. Cell Biol. 16 2015 178 189 10.1038/nrm3941 25650798 · DOI
- [5]Rothbart S.B. Strahl B.D. Interpreting the language of histone and DNA modifications Biochim. Biophys. Acta - Gene Regul. Mech. 1839 2014 627 643 10.1016/j.bbagrm.2014.03.001 PMC4099259 24631868 · DOI
- [6]Zhang T. Cooper S. Brockdorff N. The interplay of histone modifications – writers that read EMBO Rep. 16 2015 1467 1481 10.15252/embr.201540945 26474904 PMC4641500 · DOI
- [7]Soares L.M. He P.C. Chun Y. Suh H. Kim T.S. Buratowski S. Determinants of histone H3K4 methylation patterns Mol. Cell 68 2017 773 785.e6 10.1016/j.molcel.2017.10.013 29129639 PMC5706784 · DOI · Paper page
- [8]Schneider R. Bannister A.J. Myers F.A. Thorne A.W. Crane-Robinson C. Kouzarides T. Histone H3 lysine 4 methylation patterns in higher eukaryotic genes Nat. Cell Biol. 6 2004 73 77 10.1038/ncb1076 14661024 · DOI
- [9]Bernstein B.E. Kamal M. Lindblad-Toh K. Bekiranov S. Bailey D.K. Huebert D.J. McMahon S. Karlsson E.K. Kulbokas E.J. Gingeras T.R. Schreiber S.L. Lander E.S. Genomic maps and comparative analysis of histone modifications in human and mouse Cell 120 2005 169 181 10.1016/j.cell.2005.01.001 15680324 · DOI
- [12]Briggs S.D. Bryk M. Strahl B.D. Cheung W.L. Davie J.K. Dent S.Y.R. Winston F. Allis C. David Histone H3 lysine 4 methylation is mediated by Set1 and required for cell growth and rDNA silencing in Saccharomyces cerevisiae Genes Dev. 15 2001 3286 3295 10.1101/gad.940201 11751634 PMC312847 · DOI
- [13]Santos-Rosa H. Schneider R. Bannister A.J. Sherriff J. Bernstein B.E. Emre N.C.T. Schreiber S.L. Mellor J. Kouzarides T. Active genes are tri-methylated at K4 of histone H3 Nature 419 2002 407 411 10.1038/nature01080 12353038 · DOI · Paper page
- [14]Shilatifard A. The COMPASS family of histone H3K4 methylases: mechanisms of regulation in development and disease pathogenesis Annu. Rev. Biochem. 81 2012 65 95 10.1146/annurev-biochem-051710-134100 22663077 PMC4010150 · DOI · Paper page
- [15]Lee J.H. Skalnik D.G. CpG-binding protein (CXXC finger protein 1) is a component of the mammalian Set1 histone H3-Lys4 methyltransferase complex, the analogue of the yeast Set1/COMPASS complex J. Biol. Chem. 280 2005 41725 41731 10.1074/jbc.M508312200 16253997 · DOI
- [16]Lee J.-H. Tate C.M. You J.-S. Skalnik D.G. Identification and characterization of the human Set1B histone H3-Lys 4 methyltransferase complex J. Biol. Chem. 282 2007 13419 13428 10.1074/jbc.M609809200 17355966 · DOI
- [17]Fitzgerald K.T. Diaz M.O. MLL2: A new mammalian member of the trx/MLL family of genes Genomics 59 1999 187 192 10.1006/geno.1999.5860 10409430 · DOI
- [18]Milne T.A. Briggs S.D. Brock H.W. Martin M.E. Gibbs D. Allis C.D. Hess J.L. MLL targets SET domain methyltransferase activity to Hox gene promoters Mol. Cell 10 2002 1107 1117 10.1016/S1097-2765(02)00741-4 12453418 · DOI
- [19]Nakamura T. Mori T. Tada S. Krajewski W. Rozovskaia T. Wassell R. Dubois G. Mazo A. Croce C.M. Canaani E. ALL-1 is a histone methyltransferase that assembles a supercomplex of proteins involved in transcriptional regulation Mol. Cell 10 2002 1119 1128 10.1016/S1097-2765(02)00740-2 12453419 · DOI
- [20]Cho Y.W. Hong T. Hong S.H. Guo H. Yu H. Kim D. Guszczynski T. Dressler G.R. Copeland T.D. Kalkum M. Ge K. PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4 methyltransferase complex J. Biol. Chem. 282 2007 20395 20406 10.1074/jbc.M701574200 17500065 PMC2729684 · DOI
- [21]Lee J.E. Wang C. Xu S. Cho Y.W. Wang L. Feng X. Baldridge A. Sartorelli V. Zhuang L. Peng W. Ge K. H3K4 mono- and di-methyltransferase MLL4 is required for enhancer activation during cell differentiation Elife 2013 2013 10.7554/eLife.01503 PMC3869375 24368734 · DOI · Paper page
- [22]Hu D. Gao X. Morgan M.A. Herz H.-M. Smith E.R. Shilatifard A. The MLL3/MLL4 branches of the COMPASS family function as major histone H3K4 monomethylases at enhancers Mol. Cell. Biol. 33 2013 4745 4754 10.1128/mcb.01181-13 24081332 PMC3838007 · DOI · Paper page
- [23]Glaser S. Lubitz S. Loveland K.L. Ohbo K. Robb L. Schwenk F. Seibler J. Roellig D. Kranz A. Anastassiadis K. Stewart A.F. The histone 3 lysine 4 methyltransferase, Mll2, is only required briefly in development and spermatogenesis Epigenetics and Chromatin 2 2009 5 10.1186/1756-8935-2-5 19348672 PMC2674429 · DOI
- [24]Hu D. Garruss A.S. Gao X. Morgan M.A. Cook M. Smith E.R. Shilatifard A. The Mll2 branch of the COMPASS family regulates bivalent promoters in mouse embryonic stem cells Nat. Struct. Mol. Biol. 20 2013 1093 1097 10.1038/nsmb.2653 23934151 PMC3805109 · DOI
- [25]Denissov S. Hofemeister H. Marks H. Kranz A. Ciotta G. Singh S. Anastassiadis K. Stunnenberg H.G. Stewart A.F. Mll2 is required for H3K4 trimethylation on bivalent promoters in embryonic stem cells, whereas Mll1 is redundant Dev 141 2014 526 537 10.1242/dev.102681 24423662 · DOI
- [26]Bledau A.S. Schmidt K. Neumann K. Hill U. Ciotta G. Gupta A. Torres D.C. Fu J. Kranz A. Stewart A.F. Anastassiadis K. The H3K4 methyltransferase Setd1a is first required at the epiblast stage, whereas Setd1b becomes essential after gastrulation Dev 141 2014 1022 1035 10.1242/dev.098152 24550110 · DOI
- [27]Fang L. Zhang J. Zhang H. Yang X. Jin X. Zhang L. Skalnik D.G. Jin Y. Zhang Y. Huang X. Li J. Wong J. H3K4 methyltransferase set1a is a key Oct4 coactivator essential for generation of Oct4 positive inner cell mass Stem Cells 34 2016 565 580 10.1002/stem.2250 26785054 · DOI
- [28]van Nuland R. Smits A.H. Pallaki P. Jansen P.W.T.C. Vermeulen M. Timmers H.T.M. Quantitative dissection and stoichiometry determination of the human SET1/MLL histone methyltransferase complexes Mol. Cell. Biol. 33 2013 2067 2077 10.1128/mcb.01742-12 23508102 PMC3647974 · DOI
- [29]Kusch T. Histone H3 lysine 4 methylation revisited Transcription 3 2012 310 314 10.4161/trns.21911 23117820 PMC3630187 · DOI
- [30]Hyun K. Jeon J. Park K. Kim J. Writing, erasing and reading histone lysine methylations Exp. Mol. Med. 49 2017 e324 10.1038/emm.2017.11 28450737 PMC6130214 · DOI · Paper page
- [31]Ng H.H. Robert F. Young R.A. Struhl K. Targeted recruitment of Set1 histone methylase by elongating pol II provides a localized mark and memory of recent transcriptional activity Mol. Cell 11 2003 709 719 10.1016/S1097-2765(03)00092-3 12667453 · DOI
- [32]Krogan N.J. Dover J. Wood A. Schneider J. Heidt J. Boateng M.A. Dean K. Ryan O.W. Golshani A. Johnston M. Greenblatt J.F. Shilatifard A. The Paf1 complex is required for histone H3 methylation by COMPASS and Dot1p: linking transcriptional elongation to histone methylation Mol. Cell 11 2003 721 729 10.1016/S1097-2765(03)00091-1 12667454 · DOI
- [33]Bochyńska A. Lüscher-Firzlaff J. Lüscher B. Modes of interaction of KMT2 histone H3 lysine 4 methyltransferase/COMPASS complexes with chromatin Cells 7 2018 17 10.3390/cells7030017 PMC5870349 29498679 · DOI
- [34]Crump N.T. Milne T.A. Why are so many MLL lysine methyltransferases required for normal mammalian development? Cell. Mol. Life Sci. 76 2019 2885 2898 10.1007/s00018-019-03143-z 31098676 PMC6647185 · DOI
- [35]Sze C.C. Shilatifard A. MLL3/MLL4/COMPASS family on epigenetic regulation of enhancer function and cancer Cold Spring Harb. Perspect. Med. 6 2016 a026427 10.1101/cshperspect.a026427 27638352 PMC5088509 · DOI · Paper page
- [36]Jeltsch A. Broche J. Bashtrykov P. Molecular processes connecting DNA methylation patterns with DNA methyltransferases and histone modifications in mammalian genomes Genes (Basel) 9 2018 566 10.3390/genes9110566 PMC6266221 30469440 · DOI
- [37]Liyanage V.R.B. Jarmasz J.S. Murugeshan N. Bigio M.R.D. Rastegar M. Davie J.R. DNA modifications: function and applications in normal and disease states Biology (Basel) 3 2014 670 723 10.3390/biology3040670 25340699 PMC4280507 · DOI
- [38]Bird A. Taggart M. Frommer M. Miller O.J. Macleod D. A fraction of the mouse genome that is derived from islands of nonmethylated, CpG-rich DNA Cell 40 1985 91 99 10.1016/0092-8674(85)90312-5 2981636 · DOI
- [39]Lister R. Pelizzola M. Dowen R.H. Hawkins R.D. Hon G. Tonti-Filippini J. Nery J.R. Lee L. Ye Z. Ngo Q.-M. Edsall L. Antosiewicz-Bourget J. Stewart R. Ruotti V. Millar a H. Thomson J. a Ren B. Ecker J.R. Human DNA methylomes at base resolution show widespread epigenomic differences Nature 462 2009 315 322 10.1038/nature08514 19829295 PMC2857523 · DOI · Paper page
- [40]Smith Z.D. Meissner A. DNA methylation: roles in mammalian development Nat. Rev. Genet. 14 2013 204 220 10.1038/nrg3354 23400093 · DOI · Paper page
- [41]Greenberg M.V.C. Bourc’his D. The diverse roles of DNA methylation in mammalian development and disease Nat. Rev. Mol. Cell Biol. 20 2019 590 607 10.1038/s41580-019-0159-6 31399642 · DOI
- [42]cheng Shen J. Rideout W.M. Jones P.A. The rate of hydrolytic deamination of 5-methylcytosine in double-stranded DNA Nucleic Acids Res. 22 1994 972 976 10.1093/nar/22.6.972 8152929 PMC307917 · DOI
- [43]Lander E.S. Linton L.M. Birren B. Nusbaum C. Zody M.C. Baldwin J. Devon K. Dewar K. Doyle M. Fitzhugh W. Funke R. Gage D. Harris K. Heaford A. Howland J. Kann L. Lehoczky J. Levine R. McEwan P. McKernan K. Meldrim J. Mesirov J.P. Miranda C. Morris W. Naylor J. Raymond C. Rosetti M. Santos R. Sheridan A. Sougnez C. Stange-Thomann N. Stojanovic N. Subramanian A. Wyman D. Rogers J. Sulston J. Ainscough R. Beck S. Bentley D. Burton J. Clee C. Carter N. Coulson A. Deadman R. Deloukas P. Dunham A. Dunham I. Durbin R. French L. Grafham D. Gregory S. Hubbard T. Humphray S. Hunt A. Jones M. Lloyd C. McMurray A. Matthews L. Mercer S. Milne S. Mullikin J.C. Mungall A. Plumb R. Ross M. Shownkeen R. Sims S. Waterston R.H. Wilson R.K. Hillier L.W. McPherson J.D. Marra M.A. Mardis E.R. Fulton L.A. Chinwalla A.T. Pepin K.H. Gish W.R. Chissoe S.L. Wendl M.C. Delehaunty K.D. Miner T.L. Delehaunty A. Kramer J.B. Cook L.L. Fulton R.S. Johnson D.L. Minx P.J. Clifton S.W. Hawkins T. Branscomb E. Predki P. Richardson P. Wenning S. Slezak T. Doggett N. Cheng J.F. Olsen A. Lucas S. Elkin C. Uberbacher E. Frazier M. Gibbs R.A. Muzny D.M. Scherer S.E. Bouck J.B. Sodergren E.J. Worley K.C. Rives C.M. Gorrell J.H. Metzker M.L. Naylor S.L. Kucherlapati R.S. Nelson D.L. Weinstock G.M. Sakaki Y. Fujiyama A. Hattori M. Yada T. Toyoda A. Itoh T. Kawagoe C. Watanabe H. Totoki Y. Taylor T. Weissenbach J. Heilig R. Saurin W. Artiguenave F. Brottier P. Bruls T. Pelletier E. Robert C. Wincker P. Rosenthal A. Platzer M. Nyakatura G. Taudien S. Rump A. Smith D.R. Doucette-Stamm L. Rubenfield M. Weinstock K. Hong M.L. Dubois J. Yang H. Yu J. Wang J. Huang G. Gu J. Hood L. Rowen L. Madan A. Qin S. Davis R.W. Federspiel N.A. Abola A.P. Proctor M.J. Roe B.A. Chen F. Pan H. Ramser J. Lehrach H. Reinhardt R. McCombie W.R. De La Bastide M. Dedhia N. Blöcker H. Hornischer K. Nordsiek G. Agarwala R. Aravind L. Bailey J.A. Bateman A. Batzoglou S. Birney E. Bork P. Brown D.G. Burge C.B. Cerutti L. Chen H.C. Church D. Clamp M. Copley R.R. Doerks T. Eddy S.R. Eichler E.E. Furey T.S. Galagan J. Gilbert J.G.R. Harmon C. Hayashizaki Y. Haussler D. Hermjakob H. Hokamp K. Jang W. Johnson L.S. Jones T.A. Kasif S. Kaspryzk A. Kennedy S. Kent W.J. Kitts P. Koonin E.V. Korf I. Kulp D. Lancet D. Lowe T.M. McLysaght A. Mikkelsen T. Moran J.V. Mulder N. Pollara V.J. Ponting C.P. Schuler G. Schultz J. Slater G. Smit A.F.A. Stupka E. Szustakowki J. Thierry-Mieg D. Thierry-Mieg J. Wagner L. Wallis J. Wheeler R. Williams A. Wolf Y.I. Wolfe K.H. Yang S.P. Yeh R.F. Collins F. Guyer M.S. Peterson J. Felsenfeld A. Wetterstrand K.A. Myers R.M. Schmutz J. Dickson M. Grimwood J. Cox D.R. Olson M.V. Kaul R. Raymond C. Shimizu N. Kawasaki K. Minoshima S. Evans G.A. Athanasiou M. Schultz R. Patrinos A. Morgan M.J. Initial sequencing and analysis of the human genome Nature 409 2001 860 921 10.1038/35057062 11237011 · DOI · Paper page
- [44]Gardiner-Garden M. Frommer M. CpG Islands in vertebrate genomes J. Mol. Biol. 196 1987 261 282 10.1016/0022-2836(87)90689-9 3656447 · DOI
- [45]Branciamore S. Chen Z.-X. Riggs A.D. Rodin S.N. CpG island clusters and pro-epigenetic selection for CpGs in protein-coding exons of HOX and other transcription factors Proc. Natl. Acad. Sci. 107 2010 15485 15490 10.1073/pnas.1010506107 20716685 PMC2932574 · DOI
- [46]Saxonov S. Berg P. Brutlag D.L. A genome-wide analysis of CpG dinucleotides in the human genome distinguishes two distinct classes of promoters Proc. Natl. Acad. Sci. U. S. A. 103 2006 1412 1417 10.1073/pnas.0510310103 16432200 PMC1345710 · DOI · Paper page
- [47]Long H.K. Sims D. Heger A. Blackledge N.P. Kutter C. Wright M.L. Grützner F. Odom D.T. Patient R. Ponting C.P. Klose R.J. Epigenetic conservation at gene regulatory elements revealed by non-methylated DNA profiling in seven vertebrates Elife 20 2013 13) 1 19 10.7554/eLife.00348 PMC3583005 23467541 · DOI
- [48]Greenfield R. Tabib A. Keshet I. Moss J. Sabag O. Goren A. Cedar H. Role of transcription complexes in the formation of the basal methylation pattern in early development Proc. Natl. Acad. Sci. U. S. A. 115 2018 10387 10391 10.1073/pnas.1804755115 30257947 PMC6187119 · DOI
- [49]Thomson J.P. Skene P.J. Selfridge J. Clouaire T. Guy J. Webb S. Kerr A.R.W. Deaton A. Andrews R. James K.D. Turner D.J. Illingworth R. Bird A. CpG islands influence chromatin structure via the CpG-binding protein Cfp1 Nature 464 2010 1082 1086 10.1038/nature08924 20393567 PMC3730110 · DOI · Paper page
- [50]Wachter E. Quante T. Merusi C. Arczewska A. Stewart F. Webb S. Bird A. Synthetic CpG islands reveal DNA sequence determinants of chromatin structure Elife 3 2014 e03397 10.7554/eLife.03397 PMC4204011 25259796 · DOI
- [51]Mendenhall E.M. Koche R.P. Truong T. Zhou V.W. Issac B. Chi A.S. Ku M. Bernstein B.E. GC-rich sequence elements recruit PRC2 in mammalian ES cells PLoS Genet. 6 2010 e1001244 10.1371/journal.pgen.1001244 PMC3000368 21170310 · DOI
- [52]Smallwood S.A. Tomizawa S.I. Krueger F. Ruf N. Carli N. Segonds-Pichon A. Sato S. Hata K. Andrews S.R. Kelsey G. Dynamic CpG island methylation landscape in oocytes and preimplantation embryos Nat. Genet. 43 2011 811 814 10.1038/ng.864 21706000 PMC3146050 · DOI
- [53]Gahurova L. Tomizawa S. ichi Smallwood S.A. Stewart-Morgan K.R. Saadeh H. Kim J. Andrews S.R. Chen T. Kelsey G. Transcription and chromatin determinants of de novo DNA methylation timing in oocytes Epigenetics and Chromatin 10 2017 25 10.1186/s13072-017-0133-5 28507606 PMC5429541 · DOI
- [54]Zhang B. Zheng H. Huang B. Li W. Xiang Y. Peng X. Ming J. Wu X. Zhang Y. Xu Q. Liu W. Kou X. Zhao Y. He W. Li C. Chen B. Li Y. Wang Q. Ma J. Yin Q. Kee K. Meng A. Gao S. Xu F. Na J. Xie W. Allelic reprogramming of the histone modification H3K4me3 in early mammalian development Nature 537 2016 553 557 10.1038/nature19361 27626382 · DOI
- [55]Dahl J.A. Jung I. Aanes H. Greggains G.D. Manaf A. Lerdrup M. Li G. Kuan S. Li B. Lee A.Y. Preissl S. Jermstad I. Haugen M.H. Suganthan R. Bjørås M. Hansen K. Dalen K.T. Fedorcsak P. Ren B. Klungland A. Broad histone H3K4me3 domains in mouse oocytes modulate maternal-to-zygotic transition Nature 537 2016 548 552 10.1038/nature19360 27626377 PMC6283663 · DOI
- [56]Hanna C.W. Taudt A. Huang J. Gahurova L. Kranz A. Andrews S. Dean W. Stewart A.F. Colomé-Tatché M. Kelsey G. MLL2 conveys transcription-independent H3K4 trimethylation in oocytes Nat. Struct. Mol. Biol. 25 2018 73 82 10.1038/s41594-017-0013-5 29323282 · DOI
- [57]Andreu-Vieyra C.V. Chen R. Agno J.E. Glaser S. Anastassiadis K. Stewart Francis A. Matzuk M.M. MLL2 is required in oocytes for bulk histone 3 lysine 4 trimethylation and transcriptional silencing PLoS Biol. 8 2010 53 54 10.1371/journal.pbio.1000453 PMC2923083 20808952 · DOI
- [58]Voo K.S. Carlone D.L. Jacobsen B.M. Flodin A. Skalnik D.G. Cloning of a mammalian transcriptional activator that binds unmethylated CpG motifs and shares a CXXC domain with DNA methyltransferase, human trithorax, and methyl-CpG binding domain protein 1 Mol.Cell Biol. 20 2000 2108 2121 10.1128/MCB.20.6.2108-2121.2000 10688657 PMC110827 · DOI
- [59]Carlone D.L. Skalnik D.G. CpG binding protein is crucial for early embryonic development Mol. Cell. Biol. 21 2001 7601 7606 10.1128/mcb.21.22.7601-7606.2001 11604496 PMC99931 · DOI
- [60]Yu C. Fan X. Sha Q.Q. Wang H.H. Li B.T. Dai X.X. Shen L. Liu J. Wang L. Liu K. Tang F. Fan H.Y. CFP1 regulates histone H3K4 trimethylation and developmental potential in mouse oocytes Cell Rep. 20 2017 1161 1172 10.1016/j.celrep.2017.07.011 28768200 · DOI
- [61]Brown D.A. Di Cerbo V. Feldmann A. Ahn J. Ito S. Blackledge N.P. Nakayama M. McClellan M. Dimitrova E. Turberfield A.H. Long H.K. King H.W. Kriaucionis S. Schermelleh L. Kutateladze T.G. Koseki H. Klose R.J. The SET1 complex selects actively transcribed target genes via multivalent interaction with CpG island chromatin Cell Rep. 20 2017 2313 2327 10.1016/j.celrep.2017.08.030 28877467 PMC5603731 · DOI
- [62]Lee J.H. Voo K.S. Skalnik D.G. Identification and characterization of the DNA binding domain of CpG-binding protein J. Biol. Chem. 276 2001 44669 44676 10.1074/jbc.M107179200 11572867 · DOI · Paper page
- [63]Xu C. Bian C. Lam R. Dong A. Min J. The structural basis for selective binding of non-methylated CpG islands by the CFP1 CXXC domain Nat. Commun. 2 2011 227 10.1038/ncomms1237 21407193 PMC3072069 · DOI · Paper page
- [64]Krauss V. Reuter G. DNA methylation in drosophila-a critical evaluation Prog. Mol. Biol. Transl. Sci 2011 Elsevier B.V 177 191 10.1016/B978-0-12-387685-0.00003-2 21507351 · DOI
- [65]Iyer L.M. Abhiman S. Aravind L. Natural history of eukaryotic DNA methylation systems Prog. Mol. Biol. Transl. Sci 2011 Elsevier B.V 25 104 10.1016/B978-0-12-387685-0.00002-0 21507349 · DOI
- [66]Birke M. Schreiner S. García-Cuéllar M.-P. Mahr K. Titgemeyer F. Slany R.K. The MT domain of the proto-oncoprotein MLL binds to CpG-containing DNA and discriminates against methylation Nucleic Acids Res. 30 2002 958 965 10.1093/nar/30.4.958 11842107 PMC100340 · DOI
- [67]Xu C. Liu K. Lei M. Yang A. Li Y. Hughes T.R. Min J. DNA sequence recognition of human CXXC domains and their structural determinants Structure 26 2018 85 95.e3 10.1016/j.str.2017.11.022 29276034 · DOI
- [68]Allen M.D. Grummitt C.G. Hilcenko C. Min S.Y. Tonkin L.M. Johnson C.M. Freund S.M. Bycroft M. Warren A.J. Solution structure of the nonmethyl-CpG-binding CXXC domain of the leukaemia-associated MLL histone methyltransferase EMBO J. 25 2006 4503 4512 10.1038/sj.emboj.7601340 16990798 PMC1589984 · DOI
- [69]Cierpicki T. Risner L.E. Grembecka J. Lukasik S.M. Popovic R. Omonkowska M. Shultis D.D. Zeleznik-Le N.J. Bushweller J.H. Structure of the MLL CXXC domain–DNA complex and its functional role in MLL-AF9 leukemia Nat. Struct. Mol. Biol. 17 2010 62 69 10.1038/nsmb.1714 20010842 PMC2908503 · DOI
- [70]Bach C. Mueller D. Buhl S. Garcia-Cuellar M.P. Slany R.K. Alterations of the CxxC domain preclude oncogenic activation of mixed-lineage leukemia 2 Oncogene 28 2009 815 823 10.1038/onc.2008.443 19060922 · DOI
- [71]Milne T.A. Kim J. Wang G.G. Stadler S.C. Basrur V. Whitcomb S.J. Wang Z. Ruthenburg A.J. Elenitoba-Johnson K.S.J. Roeder R.G. Allis C.D. Multiple interactions recruit MLL1 and MLL1 fusion proteins to the HOXA9 locus in leukemogenesis Mol. Cell 38 2010 853 863 10.1016/j.molcel.2010.05.011 20541448 PMC2902588 · DOI
- [72]Hu D. Gao X. Cao K. Morgan M.A. Mas G. Smith E.R. Volk A.G. Bartom E.T. Crispino J.D. Di Croce L. Shilatifard A. Not all H3K4 methylations are created equal: Mll2/COMPASS dependency in primordial germ cell specification Mol. Cell 65 2017 460 475.e6 10.1016/j.molcel.2017.01.013 28157506 PMC5404503 · DOI
- [73]Meyer C. Burmeister T. Gröger D. Tsaur G. Fechina L. Renneville A. Sutton R. Venn N.C. Emerenciano M. Pombo-De-Oliveira M.S. Blunck C. Barbieri Lopes B. Almeida Zuna J. Trka J. Ballerini P. Lapillonne H. De Braekeleer M. Cazzaniga G. Abascal L. Corral Van Der Velden V.H.J. Delabesse E. Park T.S. Oh S.H. Silva M.L.M. Lund-Aho T. Juvonen V. Moore A.S. Heidenreich O. Vormoor J. Zerkalenkova E. Olshanskaya Y. Bueno C. Menendez P. Teigler-Schlegel A. Zur Stadt U. Lentes J. Göhring G. Kustanovich A. Aleinikova O. Schäfer B.W. Kubetzko S. Madsen H.O. Gruhn B. Duarte X. Gameiro P. Lippert E. Bidet A. Cayuela J.M. Clappier E. Alonso C.N. Zwaan C.M. Van Den Heuvel-Eibrink M.M. Izraeli S. Trakhtenbrot L. Archer P. Hancock J. Möricke A. Alten J. Schrappe M. Stanulla M. Strehl S. Attarbaschi A. Dworzak M. Haas O.A. Panzer-Grümayer R. Sedék L. Szczepa T. Caye A. Suarez L. Cavé H. Marschalek R. The MLL recombinome of acute leukemias in 2017 Leukemia 32 2018 273 284 10.1038/leu.2017.213 28701730 PMC5808070 · DOI
- [74]Zeleznik-Le N.J. Harden A.M. Rowley J.D. 11q23 translocations split the “AT-hook” cruciform DNA-binding region and the transcriptional repression domain from the activation domain of the mixed-lineage leukemia (MLL) gene Proc. Natl. Acad. Sci. U. S. A. 91 1994 10610 10614 10.1073/pnas.91.22.10610 7938000 PMC45071 · DOI
- [75]Winters A.C. Bernt K.M. MLL-rearranged leukemias- an update on science and clinical approaches Front. Pediatr. 5 2017 10.3389/fped.2017.00004 PMC5299633 28232907 · DOI
- [76]Ayton P.M. Cleary M.L. Molecular mechanisms of leukemogenesis mediated by MLL fusion proteins Oncogene 20 2001 5695 5707 10.1038/sj.onc.1204639 11607819 · DOI
- [77]Muntean A.G. Hess J.L. The pathogenesis of mixed-lineage leukemia Annu. Rev. Pathol. Mech. Dis. 7 2012 283 301 10.1146/annurev-pathol-011811-132434 PMC3381338 22017583 · DOI
- [78]Ayton P.M. Chen E.H. Cleary M.L. Binding to nonmethylated CpG DNA is essential for target recognition, transactivation, and myeloid transformation by an MLL oncoprotein Mol. Cell. Biol. 24 2004 10470 10478 10.1128/mcb.24.23.10470-10478.2004 15542854 PMC529055 · DOI
- [79]Risner L.E. Kuntimaddi A. Lokken A.A. Achille N.J. Birch N.W. Schoenfelt K. Bushweller J.H. Zeleznik-Le N.J. Functional specificity of CpG DNA-binding CXXC domains in mixed lineage leukemia J. Biol. Chem. 288 2013 29901 29910 10.1074/jbc.M113.474858 23990460 PMC3795288 · DOI
- [80]Rozovskaia T. Ravid-Amir O. Tillib S. Getz G. Feinstein E. Agrawal H. Nagler A. Rappaport E.F. Issaeva I. Matsuo Y. Kees U.R. Lapidot T. Lo Coco F. Foa R. Mazo A. Nakamura T. Croce C.M. Cimino G. Domany E. Canaani E. Expression profiles of acute lymphoblastic and myeloblastic leukemias with ALL-1 rearrangements Proc. Natl. Acad. Sci. U. S. A. 100 2003 7853 7858 10.1073/pnas.1132115100 12782787 PMC164677 · DOI
- [81]Armstrong S.A. Staunton J.E. Silverman L.B. Pieters R. Den Boer M.L. Minden M.D. Sallan S.E. Lander E.S. Golub T.R. Korsmeyer S.J. MLL translocations specify a distinct gene expression profile that distinguishes a unique leukemia Nat. Genet. 30 2002 41 47 10.1038/ng765 11731795 · DOI
- [82]Kerry J. Godfrey L. Repapi E. Tapia M. Blackledge N.P. Ma H. Ballabio E. O’Byrne S. Ponthan F. Heidenreich O. Roy A. Roberts I. Konopleva M. Klose R.J. Geng H. Milne T.A. MLL-AF4 spreading identifies binding sites that are distinct from super-enhancers and that govern sensitivity to DOT1L inhibition in leukemia Cell Rep. 18 2017 482 495 10.1016/j.celrep.2016.12.054 28076791 PMC5263239 · DOI
- [83]Sze C.C. Cao K. Collings C.K. Marshall S.A. Rendleman E.J. Ozark P.A. Chen F.X. Morgan M.A. Wang L. Shilatifard A. Histone H3K4 methylation-dependent and -independent functions of set1A/COMPASS in embryonic stem cell self-renewal and differentiation Genes Dev. 31 2017 1732 1737 10.1101/gad.303768.117 28939616 PMC5666672 · DOI
- [84]Ruthenburg A.J. Li H. Patel D.J. David Allis C. Multivalent engagement of chromatin modifications by linked binding modules Nat. Rev. Mol. Cell Biol. 8 2007 983 994 10.1038/nrm2298 18037899 PMC4690530 · DOI
- [85]Mahadevan J. Skalnik D.G. Efficient differentiation of murine embryonic stem cells requires the binding of CXXC finger protein 1 to DNA or methylated histone H3-Lys4 Gene 594 2016 1 9 10.1016/j.gene.2016.08.048 27590438 · DOI
- [86]Eberl H.C. Spruijt C.G. Kelstrup C.D. Vermeulen M. Mann M. A map of general and specialized chromatin readers in mouse tissues generated by label-free interaction proteomics Mol. Cell 49 2013 368 378 10.1016/j.molcel.2012.10.026 23201125 · DOI · Paper page
- [87]Wang Z. Song J. Milne T.A. Wang G.G. Li H. Allis C.D. Patel D.J. Pro isomerization in MLL1 PHD3-Bromo cassette connects H3K4me readout to CyP33 and HDAC-mediated repression Cell 141 2010 1183 1194 10.1016/j.cell.2010.05.016 20541251 PMC4690531 · DOI
- [88]Chang P.Y. Hom R.A. Musselman C.A. Zhu L. Kuo A. Gozani O. Kutateladze T.G. Cleary M.L. Binding of the MLL PHD3 finger to histone H3K4me3 is required for MLL-dependent gene transcription J. Mol. Biol. 400 2010 137 144 10.1016/j.jmb.2010.05.005 20452361 PMC2886590 · DOI
- [89]Vermeulen M. Eberl H.C. Matarese F. Marks H. Denissov S. Butter F. Lee K.K. Olsen J.V. Hyman A.A. Stunnenberg H.G. Mann M. Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers Cell 142 2010 967 980 10.1016/j.cell.2010.08.020 20850016 · DOI · Paper page
- [90]Park S. Osmers U. Raman G. Schwantes R.H. Diaz M.O. Bushweller J.H. The PHD3 domain of MLL acts as a CYP33-regulated switch between MLL-mediated activation and repression Biochemistry 49 2010 6576 6586 10.1021/bi1009387 20677832 PMC2916634 · DOI
- [91]Wu M. Wang P.F. Lee J.S. Martin-Brown S. Florens L. Washburn M. Shilatifard A. Molecular regulation of H3K4 trimethylation by Wdr82, a component of human Set1/COMPASS Mol. Cell. Biol. 28 2008 7337 7344 10.1128/mcb.00976-08 18838538 PMC2593441 · DOI
- [92]Ardehali M.B. Mei A. Zobeck K.L. Caron M. Lis J.T. Kusch T. Drosophila Set1 is the major histone H3 lysine 4 trimethyltransferase with role in transcription EMBO J. 30 2011 2817 2828 10.1038/emboj.2011.194 21694722 PMC3160253 · DOI
- [93]Hallson G. Hollebakken R.E. Li T. Syrzycka M. Kim I. Cotsworth S. Fitzpatrick K.A. Sinclair D.A.R. Honda B.M. dSet1 is the main H3K4 Di- and tri-methyltransferase throughout Drosophila development Genetics 190 2012 91 100 10.1534/genetics.111.135863 22048023 PMC3249358 · DOI
- [94]Austenaa L.M.I. Barozzi I. Simonatto M. Masella S. Della Chiara G. Ghisletti S. Curina A. de Wit E. Bouwman B.A.M. de Pretis S. Piccolo V. Termanini A. Prosperini E. Pelizzola M. de Laat W. Natoli G. Transcription of mammalian cis-regulatory elements is restrained by actively enforced early termination Mol. Cell 60 2015 460 474 10.1016/j.molcel.2015.09.018 26593720 · DOI
- [95]Ebmeier C.C. Erickson B. Allen B.L. Allen M.A. Kim H. Fong N. Jacobsen J.R. Liang K. Shilatifard A. Dowell R.D. Old W.M. Bentley D.L. Taatjes D.J. Human TFIIH kinase CDK7 regulates transcription-associated chromatin modifications Cell Rep. 20 2017 1173 1186 10.1016/j.celrep.2017.07.021 28768201 PMC5564226 · DOI
- [96]Lee J.-H. Skalnik D.G. Wdr82 is a C-terminal domain-binding protein that recruits the Setd1A histone H3-Lys4 methyltransferase complex to transcription start sites of transcribed human genes Mol. Cell. Biol. 28 2008 609 618 10.1128/mcb.01356-07 17998332 PMC2223426 · DOI
- [97]Muntean A.G. Tan J. Sitwala K. Huang Y. Bronstein J. Connelly J.A. Basrur V. Elenitoba-Johnson K.S.J. Hess J.L. The PAF complex synergizes with MLL fusion proteins at HOX loci to promote leukemogenesis Cancer Cell 17 2010 609 621 10.1016/j.ccr.2010.04.012 20541477 PMC2888888 · DOI
- [99]Kim J. Kim J.A. McGinty R.K. Nguyen U.T.T. Muir T.W. Allis C.D. Roeder R.G. The n-SET domain of Set1 regulates H2B ubiquitylation-dependent H3K4 methylation Mol. Cell 49 2013 1121 1133 10.1016/j.molcel.2013.01.034 23453808 PMC3615140 · DOI
- [100]Xue H. Yao T. Cao M. Zhu G. Li Y. Yuan G. Chen Y. Lei M. Huang J. Structural basis of nucleosome recognition and modification by MLL methyltransferases Nature 573 2019 445 449 10.1038/s41586-019-1528-1 31485071 · DOI
- [101]Pavri R. Zhu B. Li G. Trojer P. Mandal S. Shilatifard A. Reinberg D. Histone H2B monoubiquitination functions cooperatively with FACT to regulate elongation by RNA polymerase II Cell 125 2006 703 717 10.1016/j.cell.2006.04.029 16713563 · DOI
- [102]Kim J. Guermah M. McGinty R.K. Lee J.S. Tang Z. Milne T.A. Shilatifard A. Muir T.W. Roeder R.G. RAD6-mediated transcription-coupled H2B ubiquitylation directly stimulates H3K4 methylation in human cells Cell 137 2009 459 471 10.1016/j.cell.2009.02.027 19410543 PMC2678028 · DOI
- [103]Hsu P.L. Shi H. Leonen C. Kang J. Chatterjee C. Zheng N. Structural basis of H2B ubiquitination-dependent H3K4 methylation by COMPASS Mol. Cell 76 2019 712 723.e4 10.1016/j.molcel.2019.10.013 31733991 PMC6948180 · DOI
- [104]Worden E.J. Zhang X. Wolberger C. Structural basis for COMPASS recognition of an H2B-ubiquitinated nucleosome Elife 9 2020 10.7554/eLife.53199 PMC7039682 31922488 · DOI
- [105]Xie W. Nagarajan S. Baumgart S.J. Kosinsky R.L. Najafova Z. Kari V. Hennion M. Indenbirken D. Bonn S. Grundhoff A. Wegwitz F. Mansouri A. Johnsen S.A. RNF40 regulates gene expression in an epigenetic context-dependent manner Genome Biol. 18 2017 32 10.1186/s13059-017-1159-5 28209164 PMC5314486 · DOI
- [106]Jung I. Kim S.K. Kim M. Han Y.M. Kim Y.S. Kim D. Lee D. H2B monoubiquitylation is a 5′-enriched active transcription mark and correlates with exon-intron structure in human cells Genome Res. 22 2012 1026 1035 10.1101/gr.120634.111 22421545 PMC3371706 · DOI
- [107]Vethantham V. Yang Y. Bowman C. Asp P. Lee J.-H. Skalnik D.G. Dynlacht B.D. Dynamic loss of H2B ubiquitylation without corresponding changes in H3K4 trimethylation during myogenic differentiation Mol. Cell. Biol. 32 2012 1044 1055 10.1128/mcb.06026-11 22252316 PMC3295016 · DOI
- [108]Lee Y.H. Ma H. Tan T.Z. Ng S.S. Soong R. Mori S. Fu X.Y. Zernicka-Goetz M. Wu Q. Protein arginine methyltransferase 6 regulates embryonic stem cell identity Stem Cells Dev. 21 2012 2613 2622 10.1089/scd.2011.0330 22455726 PMC5729635 · DOI
- [109]Bouchard C. Sahu P. Meixner M. Nötzold R.R. Rust M.B. Kremmer E. Feederle R. Hart-Smith G. Finkernagel F. Bartkuhn M. Savai Pullamsetti S. Nist A. Stiewe T. Philipsen S. Bauer U.M. Genomic location of PRMT6-dependent H3R2 methylation is linked to the transcriptional outcome of associated genes Cell Rep. 24 2018 3339 3352 10.1016/j.celrep.2018.08.052 30232013 · DOI
- [110]Guccione E. Bassi C. Casadio F. Martinato F. Cesaroni M. Schuchlautz H. Lüscher B. Amati B. Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are mutually exclusive Nature 449 2007 933 937 10.1038/nature06166 17898714 · DOI
- [111]Hyllus D. Stein C. Schnabel K. Schiltz E. Imhof A. Dou Y. Hsieh J. Bauer U.M. PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation Genes Dev. 21 2007 3369 3380 10.1101/gad.447007 18079182 PMC2113036 · DOI
- [112]Li Y. Li H. Many keys to push: diversifying the “readership” of plant homeodomain fingers Acta Biochim. Biophys. Sin. Shanghai 44 2012 28 39 10.1093/abbs/gmr117 22194011 · DOI
- [113]He C. Liu N. Xie D. Liu Y. Xiao Y. Li F. Structural basis for histone H3K4me3 recognition by the N-terminal domain of the PHD finger protein Spp1 Biochem. J. 476 2019 1957 1973 10.1042/BCJ20190091 31253666 · DOI
- [114]Vermeulen M. Mulder K.W. Denissov S. Pijnappel W.W.M.P. van Schaik F.M.A. Varier R.A. Baltissen M.P.A. Stunnenberg H.G. Mann M. Timmers H.T.M. Selective anchoring of TFIID to nucleosomes by trimethylation of histone H3 lysine 4 Cell 131 2007 58 69 10.1016/j.cell.2007.08.016 17884155 · DOI
- [115]van Ingen H. van Schaik F.M.A. Wienk H. Ballering J. Rehmann H. Dechesne A.C. Kruijzer J.A.W. Liskamp R.M.J. Timmers H.T.M. Boelens R. Structural insight into the recognition of the H3K4me3 mark by the TFIID subunit TAF3 Structure 16 2008 1245 1256 10.1016/j.str.2008.04.015 18682226 · DOI
- [116]Iberg A.N. Espejo A. Cheng D. Kim D. Michaud-Levesque J. Richard S. Bedford M.T. Arginine methylation of the histone H3 tail impedes effector binding J. Biol. Chem. 283 2008 3006 3010 10.1074/jbc.C700192200 18077460 · DOI
- [117]Stein R.S.L. Wang W. The recognition specificity of the CHD1 chromodomain with modified histone H3 peptides J. Mol. Biol. 406 2011 527 541 10.1016/j.jmb.2010.12.030 21195088 PMC3034827 · DOI
- [118]Zheng Y. Tipton J.D. Thomas P.M. Kelleher N.L. Sweet S.M.M. Site-specific human histone H3 methylation stability: fast K4me3 turnover Proteomics 14 2014 2190 2199 10.1002/pmic.201400060 24826939 PMC4184988 · DOI
- [119]Christensen J. Agger K. Cloos P.A.C. Pasini D. Rose S. Sennels L. Rappsilber J. Hansen K.H. Salcini A.E. Helin K. RBP2 belongs to a family of demethylases, specific for tri-and dimethylated lysine 4 on histone 3 Cell 128 2007 1063 1076 10.1016/j.cell.2007.02.003 17320161 · DOI
- [120]Iwase S. Lan F. Bayliss P. de la Torre-Ubieta L. Huarte M. Qi H.H. Whetstine J.R.R. Bonni A. Roberts T.M. Shi Y. The X-linked mental retardation gene SMCX/JARID1C defines a family of histone H3 lysine 4 demethylases Cell 128 2007 1077 1088 10.1016/j.cell.2007.02.017 17320160 · DOI
- [121]Klose R.J. Yan Q. Tothova Z. Yamane K. Erdjument-Bromage H. Tempst P. Gilliland D.G. Zhang Y. Kaelin W.G. The retinoblastoma binding protein RBP2 is an H3K4 demethylase Cell 128 2007 889 900 10.1016/j.cell.2007.02.013 17320163 · DOI
- [122]Yamane K. Tateishi K. Klose R.J. Fang J. Fabrizio L.A. Erdjument-Bromage H. Taylor-Papadimitriou J. Tempst P. Zhang Y. PLU-1 is an H3K4 demethylase involved in transcriptional repression and breast cancer cell proliferation Mol. Cell 25 2007 801 812 10.1016/j.molcel.2007.03.001 17363312 · DOI
- [123]Lee M.G. Norman J. Shilatifard A. Shiekhattar R. Physical and functional association of a trimethyl H3K4 demethylase and Ring6a/MBLR, a polycomb-like protein Cell 128 2007 877 887 10.1016/j.cell.2007.02.004 17320162 · DOI
- [124]Xhabija B. Kidder B.L. KDM5B is a master regulator of the H3K4-methylome in stem cells, development and cancer Semin. Cancer Biol. 57 2019 79 85 10.1016/j.semcancer.2018.11.001 30448242 PMC6522339 · DOI
- [125]Cloos P.A.C. Christensen J. Agger K. Helin K. Erasing the methyl mark: histone demethylases at the center of cellular differentiation and disease Genes Dev. 22 2008 1115 1140 10.1101/gad.1652908 18451103 PMC2732404 · DOI
- [126]Kooistra S.M. Helin K. Post-translational modifications: molecular mechanisms and potential functions of histone demethylases Nat. Rev. Mol. Cell Biol. 13 2012 297 311 10.1038/nrm3327 22473470 · DOI
- [127]Patsialou A. Wilsker D. Moran E. DNA-binding properties of ARID family proteins Nucleic Acids Res. 33 2005 66 80 10.1093/nar/gki145 15640446 PMC546134 · DOI
- [129]Wang G.G. Song J. Wang Z. Dormann H.L. Casadio F. Li H. Luo J.L. Patel D.J. Allis C.D. Haematopoietic malignancies caused by dysregulation of a chromatin-binding PHD finger Nature 459 2009 847 851 10.1038/nature08036 19430464 PMC2697266 · DOI
- [130]Kidder B.L. Hu G. Zhao K. KDM5B focuses H3K4 methylation near promoters and enhancers during embryonic stem cell self-renewal and differentiation Genome Biol. 15 2014 R32 10.1186/gb-2014-15-2-r32 24495580 PMC4053761 · DOI
- [131]Xie L. Pelz C. Wang W. Bashar A. Varlamova O. Shadle S. Impey S. KDM5B regulates embryonic stem cell self-renewal and represses cryptic intragenic transcription EMBO J. 30 2011 1473 1484 10.1038/emboj.2011.91 21448134 PMC3102288 · DOI
- [132]Longbotham J.E. Chio C.M. Dharmarajan V. Trnka M.J. Torres I.O. Goswami D. Ruiz K. Burlingame A.L. Griffin P.R. Fujimori D.G. Histone H3 binding to the PHD1 domain of histone demethylase KDM5A enables active site remodeling Nat. Commun. 10 2019 94 10.1038/s41467-018-07829-z 30626866 PMC6327041 · DOI
- [133]Torres I.O. Kuchenbecker K.M. Nnadi C.I. Fletterick R.J. Kelly M.J.S. Fujimori D.G. Histone demethylase KDM5A is regulated by its reader domain through a positive-feedback mechanism Nat. Commun. 6 2015 6204 10.1038/ncomms7204 25686748 PMC5080983 · DOI
- [134]Zhang Y. Yang H. Guo X. Rong N. Song Y. Xu Y. Lan W. Zhang X. Liu M. Xu Y. Cao C. The PHD1 finger of KDM5B recognizes unmodified H3K4 during the demethylation of histone H3K4me2/3 by KDM5B Protein Cell 5 2014 837 850 10.1007/s13238-014-0078-4 24952722 PMC4225485 · DOI
- [135]Albert M. Schmitz S.U. Kooistra S.M. Malatesta M. Morales Torres C. Rekling J.C. Johansen J.V. Abarrategui I. Helin K. The histone demethylase Jarid1b ensures faithful mouse development by protecting developmental genes from aberrant H3K4me3 PLoS Genet. 9 2013 e1003461 10.1371/journal.pgen.1003461 PMC3630093 23637629 · DOI
- [136]Sproul D. Meehan R.R. Genomic insights into cancer-associated aberrant CpG island hypermethylation Brief. Funct. Genomics. 12 2013 174 190 10.1093/bfgp/els063 23341493 PMC3662888 · DOI
- [137]Klutstein M. Nejman D. Greenfield R. Cedar H. DNA methylation in cancer and aging Cancer Res. 76 2016 3446 3450 10.1158/0008-5472.CAN-15-3278 27256564 · DOI · Paper page
- [138]Deaton A.M. Bird A. CpG islands and the regulation of transcription Genes Dev. 25 2011 1010 1022 10.1101/gad.2037511 21576262 PMC3093116 · DOI · Paper page
- [139]Long H.K. Blackledge N.P. Klose R.J. ZF-CxxC domain-containing proteins, CpG islands and the chromatin connection Biochem. Soc. Trans. 41 2013 727 740 10.1042/BST20130028 23697932 PMC3685328 · DOI
- [142]Singh P. Li A.X. Tran D.A. Oates N. Kang E.R. Wu X. Szabó P.E. De novo DNA methylation in the male germ line occurs by default but is excluded at sites of H3K4 methylation Cell Rep. 4 2013 205 219 10.1016/j.celrep.2013.06.004 23810559 PMC3740941 · DOI
- [143]Weber M. Hellmann I. Stadler M.B. Ramos L. Pääbo S. Rebhan M. Schübeler D. Distribution, silencing potential and evolutionary impact of promoter DNA methylation in the human genome Nat. Genet. 39 2007 457 466 10.1038/ng1990 17334365 · DOI
- [144]Ciccone D.N. Su H. Hevi S. Gay F. Lei H. Bajko J. Xu G. Li E. Chen T. KDM1B is a histone H3K4 demethylase required to establish maternal genomic imprints Nature 461 2009 415 418 10.1038/nature08315 19727073 · DOI · Paper page
- [145]Stewart K.R. Veselovska L. Kim J. Huang J. Saadeh H. Tomizawa S.I. Smallwood S.A. Chen T. Kelsey G. Dynamic changes in histone modifications precede de novo DNA methylation in oocytes Genes Dev. 29 2015 2449 2462 10.1101/gad.271353.115 26584620 PMC4691949 · DOI
- [146]Wang J. Hevi S. Kurash J.K. Lei H. Gay F. Bajko J. Su H. Sun W. Chang H. Xu G. Gaudet F. Li E. Chen T. The lysine demethylase LSD1 (KDM1) is required for maintenance of global DNA methylation Nat. Genet. 41 2009 125 129 10.1038/ng.268 19098913 · DOI
- [147]Terranova R. Agherbi H. Boned A. Meresse S. Djabali M. Histone and DNA methylation defects at Hox genes in mice expressing a SET domain-truncated form of Mll Proc. Natl. Acad. Sci. 103 2006 6629 6634 10.1073/pnas.0507425103 16618927 PMC1440589 · DOI
- [148]Hu J.L. Zhou B.O. Zhang R.R. Zhang K.L. Zhou J.Q. Xu G.L. The N-terminus of histone H3 is required for de novo DNA methylation in chromatin Proc. Natl. Acad. Sci. U. S. A. 106 2009 22187 22192 10.1073/pnas.0905767106 20018712 PMC2799746 · DOI
- [149]Gowher H. Jeltsch A. Mammalian DNA methyltransferases: new discoveries and open questions Biochem. Soc. Trans. 46 2018 1191 1202 10.1042/BST20170574 30154093 PMC6581191 · DOI
- [150]Ooi S.K.T. Qiu C. Bernstein E. Li K. Jia D. Yang Z. Erdjument-Bromage H. Tempst P. Lin S.P. Allis C.D. Cheng X. Bestor T.H. DNMT3L connects unmethylated lysine 4 of histone H3 to de novo methylation of DNA Nature 448 2007 714 717 10.1038/nature05987 17687327 PMC2650820 · DOI
- [151]Otani J. Nankumo T. Arita K. Inamoto S. Ariyoshi M. Shirakawa M. Structural basis for recognition of H3K4 methylation status by the DNA methyltransferase 3A ATRX-DNMT3-DNMT3L domain EMBO Rep. 10 2009 1235 1241 10.1038/embor.2009.218 19834512 PMC2775176 · DOI
- [152]Zhang Y. Jurkowska R. Soeroes S. Rajavelu A. Dhayalan A. Bock I. Rathert P. Brandt O. Reinhardt R. Fischle W. Jeltsch A. Chromatin methylation activity of Dnmt3a and Dnmt3a/3L is guided by interaction of the ADD domain with the histone H3 tail Nucleic Acids Res. 38 2010 4246 4253 10.1093/nar/gkq147 20223770 PMC2910041 · DOI
- [153]Noh K.M. Wang H. Kim H.R. Wenderski W. Fang F. Li C.H. Dewell S. Hughes S.H. Melnick A.M. Patel D.J. Li H. Allis C.D. Engineering of a histone-recognition domain in Dnmt3a alters the epigenetic landscape and phenotypic features of mouse ESCs Mol. Cell 59 2015 89 103 10.1016/j.molcel.2015.05.017 26073541 PMC4491196 · DOI
- [154]Chen T. Tsujimoto N. Li E. The PWWP domain of Dnmt3a and Dnmt3b is required for directing DNA methylation to the major satellite repeats at pericentric heterochromatin Mol. Cell. Biol. 24 2004 9048 9058 10.1128/mcb.24.20.9048-9058.2004 15456878 PMC517890 · DOI
- [155]Ge Y.Z. Pu M.T. Gowher H. Wu H.P. Ding J.P. Jeltsch A. Xu G.L. Chromatin targeting of de novo DNA methyltransferases by the PWWP domain J. Biol. Chem. 279 2004 25447 25454 10.1074/jbc.M312296200 14998998 · DOI
- [156]Li B.Z. Huang Z. Cui Q.Y. Song X.H. Du L. Jeltsch A. Chen P. Li G. Li E. Xu G.L. Histone tails regulate DNA methylation by allosterically activating de novo methyltransferase Cell Res. 21 2011 1172 1181 10.1038/cr.2011.92 21606950 PMC3193484 · DOI
- [157]Guo X. Wang L. Li J. Ding Z. Xiao J. Yin X. He S. Shi P. Dong L. Li G. Tian C. Wang J. Cong Y. Xu Y. Structural insight into autoinhibition and histone H3-induced activation of DNMT3A Nature 517 2015 640 644 10.1038/nature13899 25383530 · DOI · Paper page
- [158]Feng W. Yonezawa M. Ye J. Jenuwein T. Grummt I. PHF8 activates transcription of rRNA genes through H3K4me3 binding and H3K9me1/2 demethylation Nat. Struct. Mol. Biol. 17 2010 445 450 10.1038/nsmb.1778 20208542 · DOI
- [160]Pack L.R. Yamamoto K.R. Fujimori D.G. Opposing chromatin signals direct and regulate the activity of lysine demethylase 4C (KDM4C) J. Biol. Chem. 291 2016 6060 6070 10.1074/jbc.M115.696864 26747609 PMC4813556 · DOI
- [161]Lohse B. Helgstrand C. Kristensen J.B.L. Leurs U. Cloos P.A.C. Kristensen J.L. Clausen R.P. Posttranslational modifications of the histone 3 tail and their impact on the activity of histone lysine demethylases in vitro PLoS One 8 2013 e67653 10.1371/journal.pone.0067653 PMC3699631 23844048 · DOI
- [163]Bilodeau S. Kagey M.H. Frampton G.M. Rahl P.B. Young R.A. SetDB1 contributes to repression of genes encoding developmental regulators and maintenance of ES cell state Genes Dev. 23 2009 2484 2489 10.1101/gad.1837309 19884255 PMC2779743 · DOI
- [164]Wan M. Liang J. Xiong Y. Shi F. Zhang Y. Lu W. He Q. Yang D. Chen R. Liu D. Barton M. Songyang Z. The trithorax group protein Ash2l is essential for pluripotency and maintaining open chromatin in embryonic stem cells J. Biol. Chem. 288 2013 5039 5048 10.1074/jbc.M112.424515 23239880 PMC3576105 · DOI
- [165]Binda O. LeRoy G. Bua D.J. Garcia B.A. Gozani O. Richard S. Trimethylation of histone H3 lysine 4 impairs methylation of histone H3 lysine 9: regulation of lysine methyltransferases by physical interaction with their substrates Epigenetics 5 2010 767 775 10.4161/epi.5.8.13278 21124070 PMC3052887 · DOI
- [166]Qi H.H. Sarkissian M. Hu G.Q. Wang Z. Bhattacharjee A. Gordon D.B. Gonzales M. Lan F. Ongusaha P.P. Huarte M. Yaghi N.K. Lim H. Garcia B.A. Brizuela L. Zhao K. Roberts T.M. Shi Y. Histone H4K20/H3K9 demethylase PHF8 regulates zebrafish brain and craniofacial development Nature 466 2010 503 507 10.1038/nature09261 20622853 PMC3072215 · DOI
- [167]Fortschegger K. de Graaf P. Outchkourov N.S. van Schaik F.M.A. Timmers H.T.M. Shiekhattar R. PHF8 targets histone methylation and RNA polymerase II to activate transcription Mol. Cell. Biol. 30 2010 3286 3298 10.1128/mcb.01520-09 20421419 PMC2897584 · DOI
- [168]Wen H. Li J. Song T. Lu M. Kan P.Y. Lee M.G. Sha B. Shi X. Recognition of histone H3K4 trimethylation by the plant homeodomain of PHF2 modulates histone demethylation J. Biol. Chem. 285 2010 9322 9326 10.1074/jbc.C109.097667 20129925 PMC2843180 · DOI
- [169]Huang Y. Recognition of histone H3 lysine-4 methylation by the double Tudor domain of JMJD2A Science 312 2006 748 751 10.1126/science.1125162 16601153 · DOI
- [170]Kim J. Daniel J. Espejo A. Lake A. Krishna M. Xia L. Zhang Y. Bedford M.T. Tudor, MBT and chromo domains gauge the degree of lysine methylation EMBO Rep. 7 2006 397 403 10.1038/sj.embor.7400625 16415788 PMC1456902 · DOI
- [171]Lee J. Thompson J.R. Botuyan M.V. Mer G. Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor Nat. Struct. Mol. Biol. 15 2008 109 111 10.1038/nsmb1326 18084306 PMC2211384 · DOI
- [172]Nishioka K. Chuikov S. Sarma K. Erdjument-Bromage H. Allis C.D. Tempst P. Reinberg D. Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation Genes Dev. 16 2002 479 489 10.1101/gad.967202 11850410 PMC155346 · DOI
- [173]Pedersen M.T. Agger K. Laugesen A. Johansen J.V. Cloos P.A.C. Christensen J. Helin K. The demethylase JMJD2C localizes to H3K4me3-positive transcription start sites and is dispensable for embryonic development Mol. Cell. Biol. 34 2014 1031 1045 10.1128/mcb.00864-13 24396064 PMC3958041 · DOI
- [174]Voigt P. Tee W.W. Reinberg D. A double take on bivalent promoters Genes Dev. 27 2013 1318 1338 10.1101/gad.219626.113 23788621 PMC3701188 · DOI
- [175]Schmitges F.W. Prusty A.B. Faty M. Stützer A. Lingaraju G.M. Aiwazian J. Sack R. Hess D. Li L. Zhou S. Bunker R.D. Wirth U. Bouwmeester T. Bauer A. Ly-Hartig N. Zhao K. Chan H. Gu J. Gut H. Fischle W. Müller J. Thomä N.H. Histone methylation by PRC2 is inhibited by active chromatin marks Mol. Cell 42 2011 330 341 10.1016/j.molcel.2011.03.025 21549310 · DOI
- [176]Voigt P. LeRoy G. Drury W.J. Zee B.M. Son J. Beck D.B. Young N.L. Garcia B.A. Reinberg D. Asymmetrically modified nucleosomes Cell 151 2012 181 193 10.1016/j.cell.2012.09.002 23021224 PMC3498816 · DOI
- [177]Lechner C.C. Agashe N.D. Fierz B. Traceless synthesis of asymmetrically modified bivalent nucleosomes Angew. Chemie - Int. Ed. 55 2016 2903 2906 10.1002/anie.201510996 26806951 · DOI
- [178]Chen S. Jiao L. Shubbar M. Yang X. Liu X. Unique structural platforms of Suz12 dictate distinct classes of PRC2 for chromatin binding Mol. Cell 69 2018 840 852.e5 10.1016/j.molcel.2018.01.039 29499137 PMC5912153 · DOI
- [179]Zegerman P. Canas B. Pappin D. Kouzarides T. Histone H3 lysine 4 methylation disrupts binding of nucleosome remodeling and deacetylase (NuRD) repressor complex J. Biol. Chem. 277 2002 11621 11624 10.1074/jbc.C200045200 11850414 · DOI
- [180]Mansfield R.E. Musselman C.A. Kwan A.H. Oliver S.S. Garske A.L. Davrazou F. Denu J.M. Kutateladze T.G. Mackay J.P. Plant homeodomain (PHD) fingers of CHD4 are histone H3-binding modules with preference for unmodified H3K4 and methylated H3K9 J. Biol. Chem. 286 2011 11779 11791 10.1074/jbc.M110.208207 21278251 PMC3064229 · DOI
- [181]Oliver S.S. Musselman C.A. Srinivasan R. Svaren J.P. Kutateladze T.G. Denu J.M. Multivalent recognition of histone tails by the PHD fingers of CHD5 Biochemistry 51 2012 6534 6544 10.1021/bi3006972 22834704 PMC3518043 · DOI
- [182]Paul S. Kuo A. Schalch T. Vogel H. Joshua-Tor L. McCombie W.R. Gozani O. Hammell M. Mills A.A. Chd5 requires PHD-mediated histone 3 binding for tumor suppression Cell Rep. 3 2013 92 102 10.1016/j.celrep.2012.12.009 23318260 PMC3575599 · DOI
- [183]Musselman C.A. Mansfield R.E. Garske A.L. Davrazou F. Kwan A.H. Oliver S.S. O’Leary H. Denu J.M. Mackay J.P. Kutateladze T.G. Binding of the CHD4 PHD2 finger to histone H3 is modulated by covalent modifications Biochem. J. 423 2009 179 187 10.1042/BJ20090870 19624289 PMC2885444 · DOI
- [184]Musselman C.A. Ramiŕez J. Sims J.K. Mansfield R.E. Oliver S.S. Denu J.M. Mackay J.P. Wade P.A. Hagman J. Kutateladze T.G. Bivalent recognition of nucleosomes by the tandem PHD fingers of the CHD4 ATPase is required for CHD4-mediated repression Proc. Natl. Acad. Sci. U. S. A. 109 2012 787 792 10.1073/pnas.1113655109 22215588 PMC3271909 · DOI
- [185]Reynolds N. Salmon-Divon M. Dvinge H. Hynes-Allen A. Balasooriya G. Leaford D. Behrens A. Bertone P. Hendrich B. NuRD-mediated deacetylation of H3K27 facilitates recruitment of Polycomb Repressive Complex 2 to direct gene repression EMBO J. 31 2012 593 605 10.1038/emboj.2011.431 22139358 PMC3273378 · DOI
- [186]Bernstein B.E. Mikkelsen T.S. Xie X. Kamal M. Huebert D.J. Cuff J. Fry B. Meissner A. Wernig M. Plath K. Jaenisch R. Wagschal A. Feil R. Schreiber S.L. Lander E.S. A bivalent chromatin structure marks key developmental genes in embryonic stem cells Cell 125 2006 315 326 10.1016/j.cell.2006.02.041 16630819 · DOI · Paper page
- [187]Azuara V. Perry P. Sauer S. Spivakov M. Jørgensen H.F. John R.M. Gouti M. Casanova M. Warnes G. Merkenschlager M. Fisher A.G. Chromatin signatures of pluripotent cell lines Nat. Cell Biol. 8 2006 532 538 10.1038/ncb1403 16570078 · DOI
- [188]Mikkelsen T.S. Ku M. Jaffe D.B. Issac B. Lieberman E. Giannoukos G. Alvarez P. Brockman W. Kim T.K. Koche R.P. Lee W. Mendenhall E. O’Donovan A. Presser A. Russ C. Xie X. Meissner A. Wernig M. Jaenisch R. Nusbaum C. Lander E.S. Bernstein B.E. Genome-wide maps of chromatin state in pluripotent and lineage-committed cells Nature 448 2007 553 560 10.1038/nature06008 17603471 PMC2921165 · DOI · Paper page
- [189]Mas G. Blanco E. Ballaré C. Sansó M. Spill Y.G. Hu D. Aoi Y. Le Dily F. Shilatifard A. Marti-Renom M.A. Di Croce L. Promoter bivalency favors an open chromatin architecture in embryonic stem cells Nat. Genet. 50 2018 1452 1462 10.1038/s41588-018-0218-5 30224650 · DOI
- [190]Nikolov M. Stützer A. Mosch K. Krasauskas A. Soeroes S. Stark H. Urlaub H. Fischle W. Chromatin affinity purification and quantitative mass spectrometry defining the interactome of histone modification patterns Mol. Cell. Proteomics 10 2011 M110.005371 10.1074/mcp.M110.005371 PMC3226395 21836164 · DOI
- [191]Liang G. Lin J.C.Y. Wei V. Yoo C. Cheng J.C. Nguyen C.T. Weisenberger D.J. Egger G. Takai D. Gonzales F.A. Jones P.A. Distinct localization of histone H3 acetylation and H3-K4 methylation to the transcription start sites in the human genome Proc. Natl. Acad. Sci. U. S. A. 101 2004 7357 7362 10.1073/pnas.0401866101 15123803 PMC409923 · DOI
- [192]Barnes C.E. English D.M. Cowley S.M. Acetylation and Co: an expanding repertoire of histone acylations regulates chromatin and transcription Essays Biochem. 63 2019 97 107 10.1042/EBC20180061 30940741 PMC6484784 · DOI
- [193]Koutelou E. Hirsch C.L. Dent S.Y.R. Multiple faces of the SAGA complex Curr. Opin. Cell Biol. 22 2010 374 382 10.1016/j.ceb.2010.03.005 20363118 PMC2900470 · DOI
- [194]Bian C. Xu C. Ruan J. Lee K.K. Burke T.L. Tempel W. Barsyte D. Li J. Wu M. Zhou B.O. Fleharty B.E. Paulson A. Allali-Hassani A. Zhou J.Q. Mer G. Grant P.A. Workman J.L. Zang J. Min J. Sgf29 binds histone H3K4me2/3 and is required for SAGA complex recruitment and histone H3 acetylation EMBO J. 30 2011 2829 2842 10.1038/emboj.2011.193 21685874 PMC3160252 · DOI · Paper page
- [195]Clouaire T. Webb S. Bird A. Cfp1 is required for gene expression-dependent H3K4 trimethylation and H3K9 acetylation in embryonic stem cells Genome Biol. 15 2014 451 10.1186/s13059-014-0451-x 25201068 PMC4189735 · DOI
- [197]Champagne K. Kutateladze T. Structural insight into histone recognition by the ING PHD fingers Curr. Drug Targets 10 2009 432 441 10.2174/138945009788185040 19442115 PMC2740728 · DOI
- [198]Champagne K.S. Saksouk N. Peña P.V. Johnson K. Ullah M. Yang X.J. Côté J. Kutateladze T.G. The crystal structure of the ING5 PHD finger in complex with an H3K4me3 histone peptide Proteins Struct. Funct. Genet. 72 2008 1371 1376 10.1002/prot.22140 18623064 PMC2756976 · DOI
- [199]Kim S. Natesan S. Cornilescu G. Carlson S. Tonelli M. McClurg U.L. Binda O. Robson C.N. Markley J.L. Balaz S. Glass K.C. Mechanism of Histone H3K4me3 recognition by the plant homeodomain of inhibitor of growth 3 J. Biol. Chem. 291 2016 18326 18341 10.1074/jbc.M115.690651 27281824 PMC5000080 · DOI
- [200]Hung T. Binda O. Champagne K.S. Kuo A.J. Johnson K. Chang H.Y. Simon M.D. Kutateladze T.G. Gozani O. ING4 mediates crosstalk between histone H3 K4 trimethylation and H3 acetylation to attenuate cellular transformation Mol. Cell 33 2009 248 256 10.1016/j.molcel.2008.12.016 19187765 PMC2650391 · DOI
- [201]Ormaza G. Rodríguez J.A. Ibáñez de Opakua A. Merino N. Villate M. Gorroño I. Rábano M. Palmero I. Vilaseca M. Kypta R. Vivanco M.d.M. Rojas A.L. Blanco F.J. The tumor suppressor ING5 is a dimeric, bivalent recognition molecule of the histone H3K4me3 mark J. Mol. Biol. 431 2019 2298 2319 10.1016/j.jmb.2019.04.018 31026448 · DOI
- [202]Peña P.V. Davrazou F. Shi X. Walter K.L. Verkhusha V.V. Gozani O. Zhao R. Kutateladze T.G. Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2 Nature 442 2006 100 103 10.1038/nature04814 16728977 PMC3190580 · DOI
- [203]Palacios A. Muñoz I.G. Pantoja-Uceda D. Marcaida M.J. Torres D. Martín-García J.M. Luque I. Montoya G. Blanco F.J. Molecular basis of histone H3K4me3 recognition by ING4 J. Biol. Chem. 283 2008 15956 15964 10.1074/jbc.M710020200 18381289 PMC3259640 · DOI
- [204]Shi X. Hong T. Walter K.L. Ewalt M. Michishita E. Hung T. Carney D. Peña P. Lan F. Kaadige M.R. Lacoste N. Cayrou C. Davrazou F. Saha A. Cairns B.R. Ayer D.E. Kutateladze T.G. Shi Y. Côté J. Chua K.F. Gozani O. ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression Nature 442 2006 96 99 10.1038/nature04835 16728974 PMC3089773 · DOI
- [205]Peña P.V. Hom R.A. Hung T. Lin H. Kuo A.J. Wong R.P.C. Subach O.M. Champagne K.S. Zhao R. Verkhusha V.V. Li G. Gozani O. Kutateladze T.G. Histone H3K4me3 binding is required for the DNA repair and apoptotic activities of ING1 tumor suppressor J. Mol. Biol. 380 2008 303 312 10.1016/j.jmb.2008.04.061 18533182 PMC2576750 · DOI
- [206]Saksouk N. Avvakumov N. Champagne K.S. Hung T. Doyon Y. Cayrou C. Paquet E. Ullah M. Landry A.J. Côté V. Yang X.J. Gozani O. Kutateladze T.G. Côté J. HBO1 HAT complexes target chromatin throughout gene coding regions via multiple PHD finger interactions with histone H3 tail Mol. Cell 33 2009 257 265 10.1016/j.molcel.2009.01.007 19187766 PMC2677731 · DOI
- [207]Skowyra D. Zeremski M. Neznanov N. Li M. Choi Y. Uesugi M. Hauser C.A. Gu W. Gudkov A.V. Qin J. Differential Association of Products of alternative transcripts of the candidate tumor suppressor ING1 with the mSin3/HDAC1 transcriptional corepressor complex J. Biol. Chem. 276 2001 8734 8739 10.1074/jbc.M007664200 11118440 · DOI
- [208]Kuzmichev A. Zhang Y. Erdjument-Bromage H. Tempst P. Reinberg D. Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33ING1 Mol. Cell. Biol. 22 2002 835 848 10.1128/mcb.22.3.835-848.2002 11784859 PMC133546 · DOI
- [209]Doyon Y. Cayrou C. Ullah M. Landry A.J. Côté V. Selleck W. Lane W.S. Tan S. Yang X.J. Côté J. ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation Mol. Cell 21 2006 51 64 10.1016/j.molcel.2005.12.007 16387653 · DOI
200 of 256 shown
Cited by
Sorted by citations
Histone post-translational modifications - cause and consequence of genome function
Millán-Zambrano, G., Burton, A., Bannister, A. J., & Schneider, R. (2022) · Nature Reviews Genetics · doi:10.1038/s41576-022-00468-7 · Cited by 1,116 · see citing works
Nepal, C., & Andersen, J. B. (2023) · Nature Communications · doi:10.1038/s41467-023-38272-4 · Cited by 39 · see citing works
- Authors
- Hughes, A. L., Kelley, J. R., & Klose, R. J.
- Affiliations
- University of Oxford (GB)
- Corresponding author
- Klose, Robert J.
- Venue
- Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms
- Publisher
- Elsevier BV
- Published
- 2020-08
- Volume
- 1863
- Issue
- 8
- Pages
- 194567
- ISSN
- 1874-9399 (ISSN-L)
- PMC
- PMC7294231
- OpenAlex
- W3023686945
- Cited by
- 139
- References
- 11
- Citations by year
- 2026: 13 · 2025: 26 · 2024: 30 · 2023: 25 · 2022: 24 · 2021: 18 · 2020: 3
- FWCI
- 1.68
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- European Research Council
- Wellcome Trust
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chromatin Remodeling and Cancer
- Keywords
- CpG islands, H3K4 trimethylation, histone methylation, promoter, DNA methylation, chromatin regulation, transcriptional regulation, cell type-specific gene expression, histone modifications
- MeSH terms
- Animals, Chromatin, DNA-Binding Proteins, Gene Expression Regulation, Histones, Neoplasm Proteins, Promoter Regions, Genetic, Histone-Lysine N-Methyltransferase, Protein Processing, Post-Translational, Transcription, Genetic, CpG Islands, DNA Methylation, Myeloid-Lymphoid Leukemia Protein
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review