Direct Interplay among Histones, Histone Chaperones, and a Chromatin Boundary Protein in the Control of Histone Gene Expression
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In Saccharomyces cerevisiae, the histone chaperone Rtt106 binds newly synthesized histone proteins and mediates their delivery into chromatin during transcription, replication, and silencing. Rtt106 is also recruited to histone gene regulatory regions by the HIR histone chaperone complex to ensure S-phase-specific expression. Here we showed that this Rtt106:HIR complex included Asf1 and histone proteins. Mutations in Rtt106 that reduced histone binding reduced Rtt106 enrichment at histone genes, leading to their increased transcription. Deletion of the chromatin boundary element Yta7 led to increased Rtt106:H3 binding, increased Rtt106 enrichment at histone gene regulatory regions, and decreased histone gene transcription at the HTA1-HTB1 locus. These results suggested a unique regulatory mechanism in which Rtt106 sensed the level of histone proteins to maintain the proper level of histone gene transcription. The role of these histone chaperones and Yta7 differed markedly among the histone gene loci, including the two H3-H4 histone gene pairs. Defects in silencing in rtt106 mutants could be partially accounted for by Rtt106-mediated changes in histone gene repression. These studies suggested that feedback mediated by histone chaperone complexes plays a pivotal role in regulating histone gene transcription.
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Outside S phase, Rtt106 forms a repressive complex together with other histone chaperones HIR and Asf1 to recruit RSC to the histone promoters.
“Outside S phase, Rtt106 forms a repressive complex together with other histone chaperones HIR and Asf1 to recruit RSC (Remodel the Structure of Chromatin), an essential ATP-dependent chromatin-remodelling complex, to the histone promoters31–33.”
From SWI/SNF and the histone chaperone Rtt106 drive expression of the Pleiotropic Drug Resistance network genes (2022) · cites this paper as [32]
Rtt106 recruitment to the histone promoters almost completely depends on Asf1, HIR and acetylation of histone H3 at K56 (H3K56Ac), and is limited by Yta7.
“Rtt106 recruitment to the histone promoters almost completely depends on Asf1, HIR and acetylation of histone H3 at K56 (H3K56Ac), and is limited by Yta7, a bromodomain- and AAA-ATPase domain-containing boundary protein31,32,35.”
From SWI/SNF and the histone chaperone Rtt106 drive expression of the Pleiotropic Drug Resistance network genes (2022) · cites this paper as [32]
Rtt106 localises at the promoters of three out of four histone gene pairs (HTA1-HTB1, HHT1-HHF1 and HHT2-HHF2, but not HTA2-HTB2) and restricts their transcription to S phase.
“Rtt106 localises at the promoters of three out of four histone gene pairs (HTA1-HTB1, HHT1-HHF1 and HHT2-HHF2, but not HTA2-HTB2), and restricts their transcription to S phase, when new histone supply is required to package newly synthesised DNA31,32.”
From SWI/SNF and the histone chaperone Rtt106 drive expression of the Pleiotropic Drug Resistance network genes (2022) · cites this paper as [32]
Rtt106 localises at the promoter of the histone gene pair HTA1-HTB1 in S. cerevisiae.
“As expected31,32, Rtt106 localised at the promoter of the histone gene pair HTA1-HTB1 (Fig. 1a).”
From SWI/SNF and the histone chaperone Rtt106 drive expression of the Pleiotropic Drug Resistance network genes (2022) · cites this paper as [32]
In our experiments, only HHF1 mRNA was significantly increased in rtt106Δ, unlike previous reports which found additional histone genes affected.
“Regarding histone gene expression, in our experiments only HHF1 mRNA was significantly increased in rtt106Δ (Fig. 3a and Supplementary Data 3), unlike previous reports which found additional histone genes affected31,32.”
From SWI/SNF and the histone chaperone Rtt106 drive expression of the Pleiotropic Drug Resistance network genes (2022) · cites this paper as [32]
The difference in histone gene effects may reflect the fact that we prepared RNA from asynchronous cells rather than cells at specific cell-cycle stages.
“This difference may reflect the fact that we prepared RNA from asynchronous cells rather than cells at specific cell-cycle stages31,32.”
From SWI/SNF and the histone chaperone Rtt106 drive expression of the Pleiotropic Drug Resistance network genes (2022) · cites this paper as [32]
The HIR histone chaperone contributes to Rtt106 recruitment to PDRE-containing promoters.
“We observed that the HIR histone chaperone, a crucial factor for recruitment of Rtt106 to the HTA1-HTB1 promoter31,32 (Fig. 2b, hir1Δ), contributes to Rtt106 recruitment to PDRE-containing promoters, since the loss of the HIR subunit Hir1 caused a reduction of Rtt106 binding (Fig. 2a, hir1Δ).”
From SWI/SNF and the histone chaperone Rtt106 drive expression of the Pleiotropic Drug Resistance network genes (2022) · cites this paper as [32]
Yta7 limits Rtt106 binding at the PDRE-containing promoters.
“We further observed that Yta7, a boundary protein that restricts Rtt106 binding at the histone promoters31,32 (Fig. 2b, yta7Δ), limits Rtt106 binding also at the PDRE-containing promoters, as loss of Yta7 increased Rtt106 binding (Fig. 2a, yta7Δ).”
From SWI/SNF and the histone chaperone Rtt106 drive expression of the Pleiotropic Drug Resistance network genes (2022) · cites this paper as [32]
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Cites
Crystal structure of the nucleosome core particle at 2.8 Å resolution
Luger, K., Mäder, A. W., Richmond, R. K., Sargent, D. F., & Richmond, T. J. (1997) · Nature · doi:10.1038/38444 · Cited by 9,466 · see citing works
Longtine, M. S., Mckenzie, A., DeMarini, D. J., Shah, N. G., Wach, A., Brachat, A., Philippsen, P., & Pringle, J. R. (1998) · Yeast · doi:10.1002/(sici)1097-0061(199807)14:10 · Cited by 5,367 · see citing works
Transformation of yeast by lithium acetate/single-stranded carrier DNA/polyethylene glycol method
Gietz, R. D., & Woods, R. A. (2002) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(02)50957-5 · Cited by 2,890 · see citing works
Replication-Dependent Marking of DNA by PCNA Facilitates CAF-1-Coupled Inheritance of Chromatin
Shibahara, K., & Stillman, B. (1999) · Cell · doi:10.1016/s0092-8674(00)80661-3 · Cited by 697 · see citing works
A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response
Masumoto, H., Hawke, D. H., Kobayashi, R., & Verreault, A. (2005) · Nature · doi:10.1038/nature03714 · Cited by 595 · see citing works
The RCAF complex mediates chromatin assembly during DNA replication and repair
Tyler, J. K., Adams, C. R., Chen, S.-R., Kobayashi, R., Kamakaka, R. T., & Kadonaga, J. T. (1999) · Nature · doi:10.1038/990147 · Cited by 555 · see citing works
A DNA Integrity Network in the Yeast Saccharomyces cerevisiae
Pan, X., Ye, P., Yuan, D., Wang, X., Bader, J. S., & Boeke, J. D. (2006) · Cell · doi:10.1016/j.cell.2005.12.036 · Cited by 538 · see citing works
THE REGULATION OF HISTONE SYNTHESIS IN THE CELL CYCLE
Osley, M. A. (1991) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.60.070191.004143 · Cited by 497 · see citing works
Structural Basis for the Histone Chaperone Activity of Asf1
English, C. M., Adkins, M. W., Carson, J. J., Churchill, M. E. A., & Tyler, J. K. (2006) · Cell · doi:10.1016/j.cell.2006.08.047 · Cited by 449 · see citing works
Acetylation of Histone H3 Lysine 56 Regulates Replication-Coupled Nucleosome Assembly
Li, Q., Zhou, H., Wurtele, H., Davies, B., Horazdovsky, B., Verreault, A., & Zhang, Z. (2008) · Cell · doi:10.1016/j.cell.2008.06.018 · Cited by 447 · see citing works
Yeast Rtt109 Promotes Genome Stability by Acetylating Histone H3 on Lysine 56
Driscoll, R., Hudson, A., & Jackson, S. P. (2007) · Science · doi:10.1126/science.1135862 · Cited by 439 · see citing works
Rtt109 Acetylates Histone H3 Lysine 56 and Functions in DNA Replication
Han, J., Zhou, H., Horazdovsky, B. F., Zhang, K., Xu, R.-M., & Zhang, Z. (2007) · Science · doi:10.1126/science.1133234 · Cited by 421 · see citing works
Acetylation in Histone H3 Globular Domain Regulates Gene Expression in Yeast
Xu, F., Zhang, K., & Grunstein, M. R. (2005) · Cell · doi:10.1016/j.cell.2005.03.011 · Cited by 394 · see citing works
Histone chaperones: an escort network regulating histone traffic
de Koning, L., Corpet, A., Haber, J. E., & Almouzni, G. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1318 · Cited by 365 · see citing works
Gunjan, A., & Verreault, A. (2003) · Cell · doi:10.1016/s0092-8674(03)00896-1 · Cited by 325 · see citing works
Celic, I., Masumoto, H., Griffith, W. P., Meluh, P. B., Cotter, R. J., Boeke, J. D., & Verreault, A. (2006) · Current Biology · doi:10.1016/j.cub.2006.06.023 · Cited by 291 · see citing works
Structure and function of the histone chaperone CIA/ASF1 complexed with histones H3 and H4
Natsume, R., Eitoku, M., Akai, Y., Sano, N., Horikoshi, M., & Senda, T. (2007) · Nature · doi:10.1038/nature05613 · Cited by 291 · see citing works
Histone H3-K56 Acetylation Is Catalyzed by Histone Chaperone-Dependent Complexes
Tsubota, T., Berndsen, C., Erkmann, J. A., Smith, C. L., Yang, L., Freitas, M. A., Denu, J. M., & Kaufman, P. D. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.02.006 · Cited by 278 · see citing works
Genome-wide location and regulated recruitment of the RSC nucleosome-remodeling complexPreprint
Ng, H., Robert, F., Young, R. A., & Struhl, K. (2002) · Genes & Development · doi:10.1101/gad.978902 · Cited by 275 · see citing works
Yeast histone deposition protein Asf1p requires Hir proteins and PCNA for heterochromatic silencing
Sharp, J. A., Fouts, E. T., Krawitz, D. C., & Kaufman, P. D. (2001) · Current Biology · doi:10.1016/s0960-9822(01)00140-3 · Cited by 262 · see citing works
Cell Cycle and Checkpoint Regulation of Histone H3 K56 Acetylation by Hst3 and Hst4
Maas, N. L., Miller, K. M., DeFazio, L. G., & Toczyski, D. P. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.06.006 · Cited by 237 · see citing works
Generation of Deletion and Point Mutations with One Primer in a Single Cloning Step
Makarova, O. V., Kamberov, E. S., & Margolis, B. L. (2000) · BioTechniques · doi:10.2144/00295bm08 · Cited by 224 · see citing works
Replication-Independent Histone Deposition by the HIR Complex and Asf1
Green, E. M., Antczak, A. J., Bailey, A. O., Franco, A. A., Wu, K. J., Yates, J. R., & Kaufman, P. D. (2005) · Current Biology · doi:10.1016/j.cub.2005.10.053 · Cited by 219 · see citing works
Rtt109 Is Required for Proper H3K56 Acetylation
Schneider, J., Bajwa, P., Johnson, F. C., Bhaumik, S. R., & Shilatifard, A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.c600265200 · Cited by 209 · see citing works
Interaction between the Drosophila CAF-1 and ASF1 Chromatin Assembly Factors
Tyler, J. K., Collins, K. A., Prasad-Sinha, J., Amiott, E. A., Bulger, M., Harte, P. J., Kobayashi, R., & Kadonaga, J. T. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.19.6574-6584.2001 · Cited by 208 · see citing works
Identification of sequences in a yeast histone promoter involved in periodic transcription
Osley, M. A., Gould, J. H., Kim, S., Kane, M., & Hereford, L. M. (1986) · Cell · doi:10.1016/0092-8674(86)90285-0 · Cited by 197 · see citing works
The histone shuffle: histone chaperones in an energetic dance
Das, C., Tyler, J. K., & Churchill, M. E. A. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.04.001 · Cited by 185 · see citing works
Gelbart, M. E., Rechsteiner, T. J., Richmond, T. J., & Tsukiyama, T. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.6.2098-2106.2001 · Cited by 170 · see citing works
Kaufman, P. D., Cohen, J. L., & Osley, M. A. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.8.4793 · Cited by 168 · see citing works
Yeast ASF1 Protein Is Required for Cell Cycle Regulation of Histone Gene Transcription
Sutton, A., Bucaria, J., Osley, M. A., & Sternglanz, R. (2001) · Genetics · doi:10.1093/genetics/158.2.587 · Cited by 150 · see citing works
Proteomic and genomic characterization of chromatin complexes at a boundary
Tackett, A. J., Dilworth, D. J., Davey, M. J., O’Donnell, M. E., Aitchison, J. D., Rout, M. P., & Chait, B. T. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200502104 · Cited by 142 · see citing works
Cell Cycle– and Chaperone-Mediated Regulation of H3K56ac Incorporation in Yeast
Kaplan, T., Liu, C. L., Erkmann, J. A., Holik, J., Grunstein, M. R., Kaufman, P. D., Friedman, N., & Rando, O. J. (2008) · PLoS Genetics · doi:10.1371/journal.pgen.1000270 · Cited by 139 · see citing works
Rtt106p is a histone chaperone involved in heterochromatin-mediated silencing
Huang, S., Zhou, H., Katzmann, D., Hochstrasser, M., Atanasova, E., & Zhang, Z. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506176102 · Cited by 130 · see citing works
Structural basis for recognition of H3K56-acetylated histone H3–H4 by the chaperone Rtt106
Su, D., Hu, Q., Li, Q., Thompson, J. R., Cui, G., Fazly, A., Davies, B. A., Botuyan, M. V., Zhang, Z., & Mer, G. (2012) · Nature · doi:10.1038/nature10861 · Cited by 128 · see citing works
Osley, M. A., & Lycan, D. E. (1987) · Molecular and Cellular Biology · doi:10.1128/mcb.7.12.4204 · Cited by 124 · see citing works
Regulation of histone synthesis and nucleosome assembly
Gunjan, A., Paik, J., & Verreault, A. (2005) · Biochimie · doi:10.1016/j.biochi.2005.02.008 · Cited by 119 · see citing works
Regulation of Histone Gene Expression in Budding Yeast
Eriksson, P. R., Ganguli, D., Nagarajavel, V, & Clark, D. J. (2012) · Genetics · doi:10.1534/genetics.112.140145 · Cited by 114 · see citing works
Fillingham, J., Kainth, P., Lambert, J.-P., van Bakel, H., Tsui, K., Peña-Castillo, L., Nislow, C., Figeys, D., Hughes, T. R., Greenblatt, J., et al. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.06.023 · Cited by 108 · see citing works
A Role for Transcriptional Repressors in Targeting the Yeast Swi/Snf Complex
Dimova, D., Nackerdien, Z., Furgeson, S., Eguchi, S., & Osley, M. A. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80189-6 · Cited by 105 · see citing works
Prochasson, P., Florens, L. A., Swanson, S. K., Washburn, M. P., & Workman, J. L. (2005) · Genes & Development · doi:10.1101/gad.1341105 · Cited by 104 · see citing works
Adkins, M. W., Carson, J. J., English, C. M., Ramey, C. J., & Tyler, J. K. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m608025200 · Cited by 91 · see citing works
Dollard, C. A., Ricupero‐Hovasse, S. L., Natsoulis, G., Boeke, J. D., & Winston, F. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.8.5223 · Cited by 87 · see citing works
Xu, H., Kim, U. J., Schuster, T., & Grunstein, M. R. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.11.5249 · Cited by 83 · see citing works
Clemente‐Ruiz, M., González‐Prieto, R., & Prado, F. (2011) · PLoS Genetics · doi:10.1371/journal.pgen.1002376 · Cited by 82 · see citing works
A novel role for histone chaperones CAF‐1 and Rtt106p in heterochromatin silencing
Huang, S., Zhou, H., Tarara, J., & Zhang, Z. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601670 · Cited by 77 · see citing works
Defining the budding yeast chromatin‐associated interactome
Lambert, J., Fillingham, J., Siahbazi, M., Greenblatt, J., Baetz, K., & Figeys, D. (2010) · Molecular Systems Biology · doi:10.1038/msb.2010.104 · Cited by 69 · see citing works
Imbeault, D., Gamar, L., Rufiange, A., Paquet, E., & Nourani, A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.c800147200 · Cited by 66 · see citing works
Antczak, A. J., Tsubota, T., Kaufman, P. D., & Berger, J. M. (2006) · BMC Structural Biology · doi:10.1186/1472-6807-6-26 · Cited by 64 · see citing works
Jambunathan, N., Martinez, A. W., Robert, E., Agochukwu, N. B., Ibos, M. E., Dugas, S. L., & Donze, D. (2005) · Genetics · doi:10.1534/genetics.105.046938 · Cited by 64 · see citing works
Silva, A. C., Xu, X., Kim, H. S., Fillingham, J., Kislinger, T., Mennella, T. A., & Keogh, M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.316489 · Cited by 60 · see citing works
Bonner, W. M., Wu, R. S., Panusz, H., & Muneses, C. (1988) · Biochemistry · doi:10.1021/bi00417a052 · Cited by 59 · see citing works
Histone Chaperone Rtt106 Promotes Nucleosome Formation Using (H3-H4)2 Tetramers
Fazly, A., Li, Q., Hu, Q., Mer, G., Horazdovsky, B. F., & Zhang, Z. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.347450 · Cited by 56 · see citing works
Two surfaces on the histone chaperone Rtt106 mediate histone binding, replication, and silencing
Zunder, R. M., Antczak, A. J., Berger, J. M., & Rine, J. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1119095109 · Cited by 48 · see citing works
Self-citationSaccharomyces cerevisiae Yta7 Regulates Histone Gene Expression
Gradolatto, A., Rogers, R. S., Lavender, H. F., Taverna, S. D., Allis, C. D., Aitchison, J. D., & Tackett, A. J. (2008) · Genetics · doi:10.1534/genetics.107.086520 · Cited by 45 · see citing works
Direct regulation of nucleosome density by the conserved AAA-ATPase Yta7
Lombardi, L. M., Ellahi, A., & Rine, J. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1116819108 · Cited by 43 · see citing works
Self-citationKurat, C. F., Lambert, J.-P., van Dyk, D., Tsui, K., van Bakel, H., Kaluarachchi, S., Friesen, H., Kainth, P., Nislow, C., Figeys, D., et al. (2011) · Genes & Development · doi:10.1101/gad.173427.111 · Cited by 41 · see citing works
Co-Evolution of Transcriptional Silencing Proteins and the DNA Elements Specifying Their Assembly
Zill, O. A., Scannell, D. R., Teytelman, L., & Rine, J. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000550 · Cited by 40 · see citing works
Self-citationStructural Analysis of Rtt106p Reveals a DNA Binding Role Required for Heterochromatin Silencing
Liu, Y., Huang, H., Zhou, B. O., Wang, S., Hu, Y., Li, X., Liu, J., Zang, J., Niu, L., Wu, J., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.055996 · Cited by 39 · see citing works
Gradolatto, A., Smart, S. K., Byrum, S. D., Blair, L. P., Rogers, R. S., Kolar, E. A., Lavender, H. F., Larson, S. K., Aitchison, J. D., Taverna, S. D., et al. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00160-09 · Cited by 37 · see citing works
Spt10 and Swi4 Control the Timing of Histone H2A/H2B Gene Activation in Budding Yeast
Eriksson, P. R., Ganguli, D., & Clark, D. J. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00909-10 · Cited by 32 · see citing works
Ferreira, M. E., Flaherty, K., & Prochasson, P. (2011) · PLoS ONE · doi:10.1371/journal.pone.0021113 · Cited by 21 · see citing works
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Kurat, C. F., Recht, J., Radovani, E., Durbic, T., Andrews, B., & Fillingham, J. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1443-9 · Cited by 68 · see citing works
Regulation of DNA replication-coupled histone gene expression
Mei, Q., Huang, J., Chen, W., Tang, J., Xu, C., Yu, Q., Cheng, Y., Ma, L., Yu, X., & Li, S. (2017) · Oncotarget · doi:10.18632/oncotarget.21887 · Cited by 69 · see citing works
Tscherner, M., Zwolanek, F., Jenull, S., Sedlazeck, F. J., Petryshyn, A., Frohner, I. E., Mavrianos, J., Chauhan, N., von Haeseler, A., & Kuchler, K. (2015) · PLOS Pathogens · doi:10.1371/journal.ppat.1005218 · Cited by 57 · see citing works
Cattaneo, M., Morozumi, Y., Perazza, D., Boussouar, F., Jamshidikia, M., Rousseaux, S., Verdel, A., & Khochbin, S. (2014) · Molecules and Cells · doi:10.14348/molcells.2014.0258 · Cited by 55 · see citing works
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Claude, K.-L., Bureik, D., Chatzitheodoridou, D., Adarska, P., Singh, A., & Schmoller, K. M. (2021) · Nature Communications · doi:10.1038/s41467-021-24451-8 · Cited by 54 · see citing works
Mei, Q., Xu, C., Gogol, M., Tang, J., Chen, W., Yu, X., Workman, J. L., & Li, S. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz101 · Cited by 35 · see citing works
Kurat, C. F., Lambert, J., Petschnigg, J., Friesen, H., Pawson, T. J., Rosebrock, A. P., Gingras, A., Fillingham, J., & Andrews, B. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1414024111 · Cited by 33 · see citing works
Jenull, S., Tscherner, M., Gulati, M., Nobile, C. J., Chauhan, N., & Kuchler, K. (2017) · Scientific Reports · doi:10.1038/s41598-017-08239-9 · Cited by 28 · see citing works
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Gali, V. K., Dickerson, D. R., Katou, Y., Fujiki, K., Shirahige, K., Owen‐Hughes, T., Kubota, T., & Donaldson, A. D. (2018) · PLoS Genetics · doi:10.1371/journal.pgen.1007783 · Cited by 21 · see citing works
Shahnejat‐Bushehri, S., & Ehrenhofer‐Murray, A. E. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1917814117 · Cited by 20 · see citing works
Nikolov, V. N., Malavia, D., & Kubota, T. (2022) · Nature Communications · doi:10.1038/s41467-022-29591-z · Cited by 16 · see citing works
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Self-citationBhagwat, M., Nagar, S., Kaur, P., Mehta, R., Vancurova, I., & Vančura, A. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101246 · Cited by 16 · see citing works
Sun, Y., Gadoury, C., Hirakawa, M. P., Bennett, R. J., Harcus, D., Marcil, A., & Whiteway, M. S. (2016) · mBio · doi:10.1128/mbio.00465-16 · Cited by 16 · see citing works
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Chacin, E., Bansal, P., Reußwig, K.-U., Díaz-Santín, L. M., Ortega, P., Vizjak, P., Gómez‐González, B., Mueller‐Planitz, F., Aguilera, A., Pfander, B., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-25424-7 · Cited by 14 · see citing works
Eustice, M., & Pillus, L. (2014) · Genetics · doi:10.1534/genetics.113.158824 · Cited by 11 · see citing works
Dewari, P. S., & Bhargava, P. (2014) · PLoS ONE · doi:10.1371/journal.pone.0108652 · Cited by 11 · see citing works
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Encinas-García, T., Loreto-Quiroz, D., Mendoza-Cano, F., Peña‐Rodríguez, A., Fimbres-Olivarría, D., Fimbres-Olivarría, D., & Sánchez‐Paz, A. (2019) · Diseases of Aquatic Organisms · doi:10.3354/dao03428 · Cited by 7 · see citing works
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Deposition of CENP-ACse4 is enhanced by mutations in the AAA+ ATPase domain of ATAD2Yta7
Kaur, N., Cho, C., Samel‐Pommerencke, A., Shahnejat‐Bushehri, S., Possling, A., Kuznecova, J., Song, J., & Ehrenhofer‐Murray, A. E. (2026) · Genetics · doi:10.1093/genetics/iyag035
- Authors
- Zunder, R. M., & Rine, J.
- Affiliations
- QB3 (US)
- ORCID
- Rine, Jasper
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2012-11
- Volume
- 32
- Issue
- 21
- Pages
- 4337-4349
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- PMC
- PMC3486138
- OpenAlex
- W2140585143
- Cited by
- 22
- References
- 61
- Citations by year
- 2026: 1 · 2023: 2 · 2022: 1 · 2021: 3 · 2020: 1 · 2019: 2 · 2018: 1 · 2017: 2 · 2016: 1 · 2015: 1 · 2014: 5 · 2013: 2
- FWCI
- 1.03
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Molecular and Cellular Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Science Foundation
- National Institutes of Health (GM31105)
- National Institute of General Medical Sciences (GM31105, R01GM031105, R37GM031105)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Keywords
- histone gene transcription, histone chaperone, Asf1, chromatin boundaries, histone H3, histone H4, Saccharomyces cerevisiae
- MeSH terms
- Cell Cycle, Chromatin, Chromosomal Proteins, Non-Histone, Histones, Nuclear Proteins, Protein Binding, Repressor Proteins, Saccharomyces cerevisiae, Transcription, Genetic, Cell Cycle Proteins, Molecular Chaperones, Gene Silencing, Feedback, Physiological, Saccharomyces cerevisiae Proteins
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