Histone crotonylation specifically marks the haploid male germ cell gene expression program: Post‐meiotic male‐specific gene expression
Abstract
The haploid male germ cell differentiation program controls essential steps of male gametogenesis and relies partly on a significant number of sex chromosome‐linked genes. These genes need to escape chromosome‐wide transcriptional repression of sex chromosomes, which occurs during meiosis and is largely maintained in post‐meiotic cells. A newly discovered histone lysine modification, crotonylation (Kcr), marks X/Y‐linked genes that are active in post‐meiotic male germ cells. Histone Kcr, by conferring resistance to transcriptional repressors, could be a dominant element in maintaining these genes active in the globally repressive environment of haploid cell sex chromosomes. Furthermore, the same mark was found associated with post‐meiotically activated genes on autosomes. Histone Kcr therefore appears to be an indicator of the male haploid cell gene expression program and a notable element of genome programming in the post‐meiotic phases of spermatogenesis.
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Histone crotonylation plays a role in active gene expression.
“consistent with a role for histone crotonylation in active gene expression9,39.”
From Histone deacetylase (HDAC) 1 and 2 complexes regulate both histone acetylation and crotonylation in vivo (2018) · cites this paper as [39]
Cites
Tan, M., Luo, H., Lee, S., Jin, F., Yang, J. S., Montellier, E., Buchou, T., Cheng, Z., Rousseaux, S., Rajagopal, N., et al. (2011) · Cell · doi:10.1016/j.cell.2011.08.008 · Cited by 1,902 · see citing works
Self-citationDistinctive chromatin in human sperm packages genes for embryo development
Hammoud, S. S., Nix, D. A., Zhang, H., Purwar, J., Carrell, D. T., & Cairns, B. R. (2009) · Nature · doi:10.1038/nature08162 · Cited by 1,326 · see citing works
An abundance of X-linked genes expressed in spermatogonia
Wang, P. J., McCarrey, J. R., Yang, F., & Page, D. C. (2001) · Nature Genetics · doi:10.1038/86927 · Cited by 784 · see citing works
Jin, C., Zang, C., Wei, G., Cui, K., Peng, W., Zhao, K., & Felsenfeld, G. (2009) · Nature Genetics · doi:10.1038/ng.409 · Cited by 776 · see citing works
Lysine propionylation and butyrylation are novel post-translational modifications in histones
Chen, Y., Sprung, R., Tang, Y., Ball, H., Sangras, B., Kim, S. C., Falck, J. R., Peng, J., Gu, W., & Zhao, Y. (2007) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m700021-mcp200 · Cited by 764 · see citing works
Self-citationMeiotic sex chromosome inactivation
Turner, J. M. A. (2007) · Development · doi:10.1242/dev.000018 · Cited by 751 · see citing works
Repressive and active histone methylation mark distinct promoters in human and mouse spermatozoa
Brykczynska, U., Hisano, M., Erkek, S., Ramos, L., Oakeley, E. J., Roloff, T. C., Beisel, C., Schübeler, D., Stadler, M. B., & Peters, A. H. F. M. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1821 · Cited by 680 · see citing works
Unique Chromatin Remodeling and Transcriptional Regulation in Spermatogenesis
Sassone‐Corsi, P. (2002) · Science · doi:10.1126/science.1070963 · Cited by 474 · see citing works
Cooperative binding of two acetylation marks on a histone tail by a single bromodomain
Morinière, J., Rousseaux, S., Steuerwald, U., Soler-López, M., Curtet, S., Vitte, A.-L., Govin, J., Gaucher, J., Sadoul, K., Hart, D. J., et al. (2009) · Nature · doi:10.1038/nature08397 · Cited by 469 · see citing works
Self-citationPostmeiotic Sex Chromatin in the Male Germline of Mice
Namekawa, S. H., Park, P. J., Zhang, L., Shima, J. E., McCarrey, J. R., Griswold, M. D., & Lee, J. T. (2006) · Current Biology · doi:10.1016/j.cub.2006.01.066 · Cited by 396 · see citing works
The consequences of asynapsis for mammalian meiosis
Burgoyne, P. S., Mahadevaiah, S. K., & Turner, J. M. A. (2009) · Nature Reviews Genetics · doi:10.1038/nrg2505 · Cited by 367 · see citing works
Khil, P. P., Smirnova, N. A., Romanienko, P. J., & Camerini‐Otero, R. D. (2004) · Nature Genetics · doi:10.1038/ng1368 · Cited by 316 · see citing works
The mouse X chromosome is enriched for multicopy testis genes showing postmeiotic expression
Mueller, J. L., Mahadevaiah, S. K., Park, P. J., Warburton, P. E., Page, D. C., & Turner, J. M. A. (2008) · Nature Genetics · doi:10.1038/ng.126 · Cited by 305 · see citing works
Arpanahi, A., Brinkworth, M. H., Iles, D., Krawetz, S. A., Paradowska, A., Platts, A. E., Saida, M., Steger, K., Tedder, P. M. R., & Miller, D. (2009) · Genome Research · doi:10.1101/gr.094953.109 · Cited by 302 · see citing works
Histone Ubiquitination and Chromatin Remodeling in Mouse Spermatogenesis
Baarends, W. M., Hoogerbrugge, J. W., Roest, H. P., Ooms, M. P., Vreeburg, J. T. M., Hoeijmakers, J. H. J., & Grootegoed, J. A. (1999) · Developmental Biology · doi:10.1006/dbio.1998.9155 · Cited by 298 · see citing works
Nuclear compartmentalization and gene activity
Francastel, C., Schübeler, D., Martin, D. I. K., & Groudine, M. T. (2000) · Nature Reviews Molecular Cell Biology · doi:10.1038/35040083 · Cited by 297 · see citing works
Pivôt-Pajot, C., Caron, C., Govin, J., Vion, A., Rousseaux, S., & Khochbin, S. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.15.5354-5365.2003 · Cited by 286 · see citing works
Self-citationTurner, J. M. A., Mahadevaiah, S. K., Ellis, P. J. I., Mitchell, M. J., & Burgoyne, P. S. (2006) · Developmental Cell · doi:10.1016/j.devcel.2006.02.009 · Cited by 278 · see citing works
Shang, E., Nickerson, H. D., Wen, D., Wang, X., & Wolgemuth, D. J. (2007) · Development · doi:10.1242/dev.004481 · Cited by 275 · see citing works
The role of histones in chromatin remodelling during mammalian spermiogenesis
Govin, J., Caron, C., Lestrat, C., Rousseaux, S., & Khochbin, S. (2004) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.2004.04266.x · Cited by 255 · see citing works
Self-citationEpigenetic Transitions in Germ Cell Development and Meiosis
Kota, S. K., & Feil, R. (2010) · Developmental Cell · doi:10.1016/j.devcel.2010.10.009 · Cited by 252 · see citing works
van der Heijden, G. W., Derijck, A. A. H. A., Pósfai, E., Giele, M., Pelczar, P., Ramos, L., Wansink, D. G., van der Vlag, J., Peters, A. H. F. M., & de Boer, P. (2007) · Nature Genetics · doi:10.1038/ng1949 · Cited by 229 · see citing works
RNF8-Dependent Histone Modifications Regulate Nucleosome Removal during Spermatogenesis
Lu, L., Wu, J., Ye, L., Gavrilina, G. B., Saunders, T. L., & Yu, X. (2010) · Developmental Cell · doi:10.1016/j.devcel.2010.01.010 · Cited by 216 · see citing works
Zhao, M., Shirley, C. R., Hayashi, S., Marcon, L., Mohapatra, B., Suganuma, R., Behringer, R. R., Boissonneault, G., Yanagimachi, R., & Meistrich, M. L. (2004) · genesis · doi:10.1002/gene.20019 · Cited by 194 · see citing works
MDC1 directs chromosome-wide silencing of the sex chromosomes in male germ cellsPreprint
Ichijima, Y., Ichijima, M., Lou, Z., Nussenzweig, A., Camerini‐Otero, R. D., Chen, J., Andreassen, P. R., & Namekawa, S. H. (2011) · Genes & Development · doi:10.1101/gad.2030811 · Cited by 192 · see citing works
The Contribution of Nuclear Compartmentalization to Gene Regulation
Carmo‐Fonseca, M. (2002) · Cell · doi:10.1016/s0092-8674(02)00650-5 · Cited by 185 · see citing works
Khalil, A. M., Boyar, F. Z., & Driscoll, D. J. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0406325101 · Cited by 181 · see citing works
From meiosis to postmeiotic events: The secrets of histone disappearance
Gaucher, J., Reynoird, N., Montellier, E., Boussouar, F., Rousseaux, S., & Khochbin, S. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07504.x · Cited by 178 · see citing works
Self-citationThe Multicopy Gene Sly Represses the Sex Chromosomes in the Male Mouse Germline after Meiosis
Cocquet, J., Ellis, P. J. I., Yamauchi, Y., Mahadevaiah, S. K., Affara, N. A., Ward, M. A., & Burgoyne, P. S. (2009) · PLoS Biology · doi:10.1371/journal.pbio.1000244 · Cited by 168 · see citing works
DNA Damage Response During Chromatin Remodeling in Elongating Spermatids of Mice1
Leduc, F., Maquennehan, V., Nkoma, G. B., & Boissonneault, G. (2007) · Biology of Reproduction · doi:10.1095/biolreprod.107.064162 · Cited by 158 · see citing works
Utley, R. T., Lacoste, N., Jobin‐Robitaille, O., Allard, S., & Côté, J. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.18.8179-8190.2005 · Cited by 152 · see citing works
Meiotic sex chromosome inactivation in male mice with targeted disruptions of Xist
Turner, J. M. A., Mahadevaiah, S. K., Elliott, D. J., Garchon, H., Pehrson, J. R., Jaenisch, R., & Burgoyne, P. S. (2002) · Journal of Cell Science · doi:10.1242/jcs.00111 · Cited by 125 · see citing works
Greaves, I. K., Rangasamy, D., Devoy, M., Graves, J. A. M., & Tremethick, D. J. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00519-06 · Cited by 119 · see citing works
Epigenetic reprogramming of the male genome during gametogenesis and in the zygote
Rousseaux, S., Reynoird, N., Escoffier, E., Thévenon, J., Caron, C., & Khochbin, S. (2008) · Reproductive BioMedicine Online · doi:10.1016/s1472-6483(10)60456-7 · Cited by 104 · see citing works
Self-citationSystematic screen reveals new functional dynamics of histones H3 and H4 during gametogenesisPreprint
Govin, J., Dorsey, J. A., Gaucher, J., Rousseaux, S., Khochbin, S., & Berger, S. L. (2010) · Genes & Development · doi:10.1101/gad.1954910 · Cited by 103 · see citing works
Self-citationPoly(ADP-ribosyl)ation during chromatin remodeling steps in rat spermiogenesis
Meyer‐Ficca, M. L., Scherthan, H., Bürkle, A., & Meyer, R. G. (2005) · Chromosoma · doi:10.1007/s00412-005-0344-6 · Cited by 95 · see citing works
Hogeveen, K. N., & Sassone‐Corsi, P. (2006) · Human Fertility · doi:10.1080/14647270500463400 · Cited by 76 · see citing works
Moving chromatin within the interphase nucleus-controlled transitions?
Chuang, C.-H., & Belmont, A. S. (2007) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2007.08.012 · Cited by 63 · see citing works
Baarends, W. M., Wassenaar, E., Hoogerbrugge, J. W., Schoenmakers, S., Sun, Z., & Grootegoed, J. A. (2007) · Journal of Cell Science · doi:10.1242/jcs.03451 · Cited by 60 · see citing works
Nuclear organization in the 3D space of the nucleus — cause or consequence?
Núñez, E., Fu, X., & Rosenfeld, M. G. (2009) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2009.07.005 · Cited by 52 · see citing works
A new insight into male genome reprogramming by histone variants and histone code
Boussouar, F., Rousseaux, S., & Khochbin, S. (2008) · Cell Cycle · doi:10.4161/cc.7.22.6975 · Cited by 47 · see citing works
Self-citationMulugeta, E., Wassenaar, E., Hoogerbrugge, J. W., Sleddens–Linkels, E., Ooms, M. P., Sun, Z., van IJcken, W. F. J., Grootegoed, J. A., & Baarends, W. M. (2010) · BMC Genomics · doi:10.1186/1471-2164-11-367 · Cited by 41 · see citing works
Fournier, A., Leer, A. M., Lefebvre, C., Duley, S., Barki‐Celli, L., Ribeyron, J., Kassambara, A., Hamaidia, S., Granjon, A., Gressin, R., et al. (2010) · EMBO Molecular Medicine · doi:10.1002/emmm.201000067 · Cited by 38 · see citing works
Self-citationReynard, L. N., & Turner, J. M. A. (2009) · Journal of Cell Science · doi:10.1242/jcs.049916 · Cited by 27 · see citing works
Khalil, A. M., & Driscoll, D. J. (2005) · Cytogenetic and Genome Research · doi:10.1159/000087508 · Cited by 24 · see citing works
Specialization of the general transcriptional machinery in male germ cells
Kolthur‐Seetharam, U., Martianov, I., & Davidson, I. (2008) · Cell Cycle · doi:10.4161/cc.7.22.6976 · Cited by 22 · see citing works
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Cited by
Sorted by citations
Metabolic regulation of gene expression through histone acylations
Sabari, B. R., Zhang, D., Allis, C. D., & Zhao, Y. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.140 · Cited by 1,134 · see citing works
Self-citationSkakkebæk, N. E., Meyts, E. R., Louis, G. M. B., Toppari, J., Andersson, A., Eisenberg, M. L., Jensen, T. K., Jørgensen, N., Swan, S. H., Sapra, K. J., et al. (2015) · Physiological Reviews · doi:10.1152/physrev.00017.2015 · Cited by 998 · see citing works
Weinert, B. T., Scholz, C. W., Wagner, S., Iešmantavičius, V., Su, D., Daniel, J. A., & Choudhary, C. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.07.024 · Cited by 757 · see citing works
Interpreting the language of histone and DNA modifications
Rothbart, S. B., & Strahl, B. D. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.03.001 · Cited by 721 · see citing works
Chromatin dynamics during spermiogenesis
Rathke, C., Baarends, W. M., Awe, S., & Renkawitz‐Pohl, R. (2013) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2013.08.004 · Cited by 548 · see citing works
Lysine 2-hydroxyisobutyrylation is a widely distributed active histone mark
Dai, L., Peng, C., Montellier, E., Lu, Z., Chen, Y., Ishii, H., Debernardi, A., Buchou, T., Rousseaux, S., Jin, F., et al. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1497 · Cited by 460 · see citing works
Self-citationMolecular Coupling of Histone Crotonylation and Active Transcription by AF9 YEATS Domain
Li, Y., Sabari, B. R., Panchenko, T., Wen, H., Zhao, D., Guan, H., Wan, L., Huang, H., Tang, Z., Zhao, Y., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.03.028 · Cited by 384 · see citing works
Self-citationSIRT5 promotes IDH2 desuccinylation and G6PD deglutarylation to enhance cellular antioxidant defense
Zhou, L., Wang, F., Sun, R., Chen, X., Zhang, M., Xu, Q., Wang, Y., Wang, S., Xiong, Y., Guan, K., et al. (2016) · EMBO Reports · doi:10.15252/embr.201541643 · Cited by 290 · see citing works
Epigenetic regulation of the histone-to-protamine transition during spermiogenesis
Bao, J., & Bedford, M. T. (2016) · Reproduction · doi:10.1530/rep-15-0562 · Cited by 275 · see citing works
Liu, R., Wu, J., Guo, H., Yao, W., Li, S., Lu, Y., Jia, Y., Liang, X., Tang, J., & Zhang, H. (2023) · MedComm · doi:10.1002/mco2.292 · Cited by 287 · see citing works
Goudarzi, A., Zhang, D., Huang, H., Barral, S., Kwon, O. K., Qi, S., Tang, Z., Buchou, T., Vitte, A.-L., Tie-ming, H., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.03.014 · Cited by 264 · see citing works
Self-citationChromatin-to-nucleoprotamine transition is controlled by the histone H2B variant TH2BPreprint
Montellier, E., Boussouar, F., Rousseaux, S., Zhang, K., Buchou, T., Fenaille, F., Shiota, H., Debernardi, A., Héry, P., Curtet, S., et al. (2013) · Genes & Development · doi:10.1101/gad.220095.113 · Cited by 236 · see citing works
Self-citationCharacterization of histone acylations links chromatin modifications with metabolism
Simithy, J., Sidoli, S., Yuan, Z., Coradin, M., Bhanu, N. V., Marchione, D. M., Klein, B. J., Bazilevsky, G. A., McCullough, C. E., Magin, R. S., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-01384-9 · Cited by 226 · see citing works
YEATS2 is a selective histone crotonylation reader
Zhao, D. Y., Guan, H., Zhao, S., Mi, W., Wen, H., Li, Y., Zhao, Y., Allis, C. D., Shi, X., & Li, H. (2016) · Cell Research · doi:10.1038/cr.2016.49 · Cited by 224 · see citing works
Self-citationBeyond histone acetylation—writing and erasing histone acylations
Zhao, S., Zhang, X., & Li, H. (2018) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2018.10.001 · Cited by 207 · see citing works
Epigenetics and its role in male infertility
Dada, R., Kumar, M., Jesudasan, R. A., Fernández, J. L., Gosálvez, J., & Agarwal, A. K. (2012) · Journal of Assisted Reproduction and Genetics · doi:10.1007/s10815-012-9715-0 · Cited by 208 · see citing works
Selective recognition of histone crotonylation by double PHD fingers of MOZ and DPF2
Xiong, X., Panchenko, T., Yang, S., Zhao, S., Yan, P., Zhang, W., Xie, W., Li, Y., Zhao, Y., Allis, C. D., et al. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2218 · Cited by 192 · see citing works
Self-citationLarge-Scale Identification of Protein Crotonylation Reveals Its Role in Multiple Cellular Functions
Wei, W., Mao, A., Tang, B., Zeng, Q., Gao, S., Liu, X., Lu, L., Li, W., Du, J. X., Li, J., et al. (2017) · Journal of Proteome Research · doi:10.1021/acs.jproteome.7b00012 · Cited by 163 · see citing works
Proteomic characterization of novel histone post-translational modifications
Arnaudo, A. M., & Garcia, B. A. (2013) · Epigenetics & Chromatin · doi:10.1186/1756-8935-6-24 · Cited by 161 · see citing works
Histone crotonylation promotes mesoendodermal commitment of human embryonic stem cells
Fang, Y., Xu, X., Ding, J., Yang, L., Doan, M. T., Karmaus, P. W. F., Snyder, N. W., Zhao, Y., Li, J., & Li, X. (2021) · Cell stem cell · doi:10.1016/j.stem.2020.12.009 · Cited by 158 · see citing works
Self-citationYang, M., Wang, Y., Chen, Y., Cheng, Z., Gu, J., Deng, J., Bi, L., Chen, C., Mo, R., Wang, X., et al. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m114.045922 · Cited by 139 · see citing works
Kelly, R. D. W., Chandru, A., Watson, P. J., Song, Y., Blades, M., Robertson, N. S., Jamieson, A. G., Schwabe, J. W. R., & Cowley, S. M. (2018) · Scientific Reports · doi:10.1038/s41598-018-32927-9 · Cited by 138 · see citing works
Protein Acetylation and Its Role in Bacterial Virulence
Ren, J., Sang, Y., Lu, J. L., & Yao, Y.-F. (2017) · Trends in Microbiology · doi:10.1016/j.tim.2017.04.001 · Cited by 133 · see citing works
YEATS Domain—A Histone Acylation Reader in Health and Disease
Zhao, D. Y., Li, Y., Xiong, X., Chen, Z., & Li, H. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.03.010 · Cited by 133 · see citing works
Epigenetic disorders and male subfertility
Chalas, C., Jouannet, P., & Jammes, H. (2013) · Fertility and Sterility · doi:10.1016/j.fertnstert.2013.01.124 · Cited by 127 · see citing works
The Regulation and Function of Histone Crotonylation
Ntorla, A., & Burgoyne, J. R. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.624914 · Cited by 107 · see citing works
Sun, H., Liu, X., Li, F., Li, W., Zhang, J., Xiao, Z., Shen, L., Li, Y., Wang, F., & Yang, J. (2017) · Scientific Reports · doi:10.1038/s41598-017-03369-6 · Cited by 94 · see citing works
Fu, Y., Yu, J., Li, F., & Ge, S. (2022) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-022-02338-w · Cited by 96 · see citing works
Human sperm chromatin epigenetic potential: genomics, proteomics, and male infertility
Oliva, R., Castillo, J., Estanyol, J. M., & Ballescà, J. (2015) · Asian Journal of Andrology · doi:10.4103/1008-682x.153302 · Cited by 92 · see citing works
Sex chromosome inactivation in germ cells: emerging roles of DNA damage response pathways
Ichijima, Y., Sin, H., & Namekawa, S. H. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-0941-5 · Cited by 88 · see citing works
Gattner, M. J., Vrábel, M., & Carell, T. (2012) · Chemical Communications · doi:10.1039/c2cc37836a · Cited by 89 · see citing works
Liu, S., Xue, C., Fang, Y., Chen, G., Peng, X., Zhou, Y., Chen, C., Liu, G., Gu, M., Wang, K., et al. (2018) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra118.000640 · Cited by 88 · see citing works
Modulating Lysine Crotonylation in Cardiomyocytes Improves Myocardial Outcomes
Cai, W., Xu, D., Zeng, C., Liao, F., Li, R., Lin, Y., Zhao, Y., Dong, W., Wang, Q., Yang, H., et al. (2022) · Circulation Research · doi:10.1161/circresaha.122.321054 · Cited by 86 · see citing works
Self-citationMeiotic Sex Chromosome Inactivation Is Disrupted in Sterile Hybrid Male House Mice
Polly Campbell, A., Good, J. M., & Nachman, M. W. (2013) · Genetics · doi:10.1534/genetics.112.148635 · Cited by 82 · see citing works
Huang, H., Wang, D., & Zhao, Y. (2018) · PROTEOMICS · doi:10.1002/pmic.201700230 · Cited by 83 · see citing works
Self-citationProtein lysine de-2-hydroxyisobutyrylation by CobB in prokaryotes
Dong, H., Zhai, G., Chen, C., Bai, X. F., Tian, S., Hu, D., Fan, E., & Zhang, K. (2019) · Science Advances · doi:10.1126/sciadv.aaw6703 · Cited by 80 · see citing works
Dhar, S., Thota, A., & Rao, M. R. S. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.288167 · Cited by 80 · see citing works
The Expanding Constellation of Histone Post-Translational Modifications in the Epigenetic Landscape
Cavalieri, V. (2021) · Genes · doi:10.3390/genes12101596 · Cited by 80 · see citing works
Histone Acylation beyond Acetylation: Terra Incognita in Chromatin Biology.
Rousseaux, S., & Khochbin, S. (2015) · PubMed Central · doi:10.22074/cellj.2015.506 · Cited by 73 · see citing works
Self-citationHistone crotonylation-centric gene regulation
Li, K., & Wang, Z. (2021) · Epigenetics & Chromatin · doi:10.1186/s13072-021-00385-9 · Cited by 73 · see citing works
Krone, M. W., Travis, C. R., Lee, G. Y., Eckvahl, H. J., Houk, K. N., & Waters, M. L. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.0c06568 · Cited by 58 · see citing works
The Function and related Diseases of Protein Crotonylation
Wang, S., Mu, G., Qiu, B., Wang, M., Yu, Z., Wang, W., Wang, J., & Yang, Y. (2021) · International Journal of Biological Sciences · doi:10.7150/ijbs.58872 · Cited by 54 · see citing works
Chen, Y., Wang, Z., Wang, Y., Ying, G., Chen, Z., & Song, J. (2021) · Briefings in Bioinformatics · doi:10.1093/bib/bbab146 · Cited by 54 · see citing works
Systematic Identification of Lysine 2-hydroxyisobutyrylated Proteins in Proteus mirabilis
Dong, H., Guo, Z., Feng, W., Zhang, T., Zhai, G., Palusiak, A., Różalski, A., Tian, S., Bai, X., Shen, L., et al. (2018) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra117.000430 · Cited by 52 · see citing works
Metabolism-driven chromatin dynamics: Molecular principles and technological advances
Sahu, V., & Lü, C. (2025) · Molecular Cell · doi:10.1016/j.molcel.2024.12.012 · Cited by 54 · see citing works
Comptour, A., Moretti, C., Serrentino, M., Auer, J., Ialy‐Radio, C., Ward, M. A., Touré, A., Vaiman, D., & Cocquet, J. (2014) · FEBS Journal · doi:10.1111/febs.12724 · Cited by 48 · see citing works
YEATS domain: Linking histone crotonylation to gene regulation
Li, Y., Zhao, D. Y., Chen, Z., & Li, H. (2016) · Transcription · doi:10.1080/21541264.2016.1239602 · Cited by 48 · see citing works
Moretti, C., Serrentino, M., Ialy‐Radio, C., Delessard, M., Soboleva, T., Torès, F., Leduc, M., Nitschké, P., Drevet, J. R., Tremethick, D. J., et al. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2017.32 · Cited by 45 · see citing works
Post-Translational Modification of Proteins in Toxicological Research: Focus on Lysine Acylation
Lee, S. (2013) · Toxicological Research · doi:10.5487/tr.2013.29.2.081 · Cited by 43 · see citing works
Emerging roles of non-histone protein crotonylation in biomedicine
Hou, J., Zhou, L., Li, J., Wang, D., & Cao, J. (2021) · Cell & Bioscience · doi:10.1186/s13578-021-00616-2 · Cited by 44 · see citing works
Novel O-GlcNAcylation on Ser40 of canonical H2A isoforms specific to viviparity
Hirosawa, M., Hayakawa, K., Yoneda, C., Arai, D., Shiota, H., Suzuki, T., Tanaka, S., Dohmae, N., & Shiota, K. (2016) · Scientific Reports · doi:10.1038/srep31785 · Cited by 43 · see citing works
Expression and epigenomic landscape of the sex chromosomes in mouse post-meiotic male germ cells
Moretti, C., Vaiman, D., Torès, F., & Cocquet, J. (2016) · Epigenetics & Chromatin · doi:10.1186/s13072-016-0099-8 · Cited by 41 · see citing works
The Contribution of Histone Crotonylation to Tissue Health and Disease: Focus on Kidney Health
Martinez-Moreno, J. M., Fontecha‐Barriuso, M., Martín‐Sánchez, D., Sánchez-Niño, M. D., Ruiz‐Ortega, M., Sanz, A. B., & Ortíz, A. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.00393 · Cited by 41 · see citing works
Fu, J., Li, Y., Wang, L., Zhen, L., Yang, Q., Li, P., & Li, X. (2017) · Theriogenology · doi:10.1016/j.theriogenology.2017.07.020 · Cited by 39 · see citing works
Crotonylation and disease: Current progress and future perspectives
Yang, P., Qin, Y., Zeng, L., He, Y., Xie, Y., Cheng, X., Huang, W. G., & Cao, L. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115108 · Cited by 38 · see citing works
Gaviard, C., Cosette, P., Jouenne, T., & Hardouin, J. (2019) · Journal of Proteome Research · doi:10.1021/acs.jproteome.8b00556 · Cited by 37 · see citing works
Boussouar, F., Goudarzi, A., Buchou, T., Shiota, H., Barral, S., Debernardi, A., Guardiola, P., Brindle, P. K., Martinez, G., Arnoult, C., et al. (2014) · Andrology · doi:10.1111/j.2047-2927.2014.00184.x · Cited by 36 · see citing works
Self-citationP300 regulates histone crotonylation and preimplantation embryo development
Gao, D., Li, C., Liu, S., Xu, T., Lin, X., Tan, Y.-P., Gao, F.-M., Yi, L.-T., Zhang, J. V., Ma, J., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-50731-0 · Cited by 34 · see citing works
Zhao, Y., He, N., Chen, Z., & Li, L. (2020) · IEEE Access · doi:10.1109/access.2020.2966592 · Cited by 33 · see citing works
Self-citationLuo, Y., Zhuan, Q., Li, J., Du, X., Huang, Z., Hou, Y., & Fu, X. (2020) · Reproductive Sciences · doi:10.1007/s43032-020-00241-3 · Cited by 32 · see citing works
Aravind, L., Burroughs, A. M., Zhang, D., & Iyer, L. M. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a016063 · Cited by 30 · see citing works
Xue, C., Qiao, Z., Chen, X., Cao, P., Liu, K., Liu, S., Lu, Y., & Gong, Z. (2020) · Rice · doi:10.1186/s12284-020-00389-1 · Cited by 29 · see citing works
Crystal structure of the nucleosome containing histone H3 with crotonylated lysine 122
Suzuki, Y., Horikoshi, N., Kato, D., & Kurumizaka, H. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.12.041 · Cited by 28 · see citing works
The Response of Rhodotorula mucilaginosa to Patulin Based on Lysine Crotonylation
Yang, Q., Li, Y., Apaliya, M. T., Zheng, X., Boateng, N. A. S., Zhang, X., & Zhang, H. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.02025 · Cited by 27 · see citing works
Zhou, X., Song, N., Li, D., Li, X., & Liu, W. (2021) · mSystems · doi:10.1128/msystems.01316-20 · Cited by 27 · see citing works
The crosstalking of lactate‐Histone lactylation and tumor
Rong, Y., Dong, F., Zhang, G., Tang, M., Zhao, X., Zhang, Y., Tao, P., & Cai, H. (2023) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.202200102 · Cited by 26 · see citing works
Hundertmark, T., Gärtner, S. M. K., Rathke, C., & Renkawitz‐Pohl, R. (2018) · PLoS ONE · doi:10.1371/journal.pone.0203622 · Cited by 25 · see citing works
Dou, L., Zhang, Z., Xu, L., & Zou, Q. (2022) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2022.06.032 · Cited by 23 · see citing works
Lin, H., Tang, D., Xu, Y. J., Zhang, R., Ou, M., Zheng, F., Chen, J., Zhang, Y., Zou, G., Xue, W., et al. (2020) · Molecular Medicine Reports · doi:10.3892/mmr.2020.10931 · Cited by 22 · see citing works
DOT1L regulates chromatin reorganization and gene expression during sperm differentiation
Blanco, M., Khattabi, L. E., Gobé, C., Crespo, M., Coulée, M., de la Iglesia, A., Ialy‐Radio, C., Lapoujade, C., Givelet, M., Delessard, M., et al. (2023) · EMBO Reports · doi:10.15252/embr.202256316 · Cited by 22 · see citing works
An Update on Lysine Deacylases Targeting the Expanding “Acylome”
Olsen, C. A. (2013) · ChemMedChem · doi:10.1002/cmdc.201300421 · Cited by 19 · see citing works
Structural Basis for the Site-Specific Incorporation of Lysine Derivatives into Proteins
Flügel, V., Vrábel, M., & Schneider, S. (2014) · PLoS ONE · doi:10.1371/journal.pone.0096198 · Cited by 19 · see citing works
Lysine crotonylation in disease: mechanisms, biological functions and therapeutic targets
Ji, Y., Liu, S., Zhang, Y., Min, Y., Wei, L., Guan, C., Yu, H., & Zhang, Z. (2025) · Epigenetics & Chromatin · doi:10.1186/s13072-025-00577-7 · Cited by 18 · see citing works
Non-Histone Lysine Crotonylation Is Involved in the Regulation of White Fat Browning
Liu, Y., Li, Y., Liang, J., Sun, Z., & Sun, C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232112733 · Cited by 18 · see citing works
Wei, X., Sha, Y., Zhao, Y., He, N., & Li, L. (2021) · IEEE Access · doi:10.1109/access.2021.3068413 · Cited by 18 · see citing works
Self-citationProtein lysine crotonylation in cellular processions and disease associations
Zhao, H., Han, Y., Zhou, P., Guan, H., & Gao, S. (2023) · Genes & Diseases · doi:10.1016/j.gendis.2023.06.029 · Cited by 17 · see citing works
Global Lysine Crotonylation Alterations of Host Cell Proteins Caused by Brucella Effector BspF
Zhu, J., Dong, Q., Dong, C., Zhang, X., Zhang, H., & Chen, Z. (2021) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2020.603457 · Cited by 17 · see citing works
The Brucella Effector Protein BspF Regulates Apoptosis through the Crotonylation of p53
Lin, R., Li, A., Li, Y., Shen, R., Du, F., Zheng, M., Zhu, J., Chen, J., Jiang, P., Zhang, H., et al. (2023) · Microorganisms · doi:10.3390/microorganisms11092322 · Cited by 12 · see citing works
Starvation promotes histone lysine butyrylation in the liver of male but not female mice
Goudarzi, A., Hosseinmardi, N., Salami, S., Mehdikhani, F., Derakhshan, S., & Aminishakib, P. (2020) · Gene · doi:10.1016/j.gene.2020.144647 · Cited by 12 · see citing works
Sirtuin activation as a therapeutic approach against inborn errors of metabolism
Bleeker, J. C., & Houtkooper, R. H. (2016) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-016-9939-8 · Cited by 11 · see citing works
Gan, Q. Y., Tang, D., Yan, Q., Chen, J., Xu, Y. J., Xue, W., Xiao, L., Zheng, F., Xu, H., Fu, Y., et al. (2021) · Canadian Respiratory Journal · doi:10.1155/2021/6652297 · Cited by 11 · see citing works
PlantNh-Kcr: a deep learning model for predicting non-histone crotonylation sites in plants
Jiang, Y., Yan, R., & Wang, X. (2024) · Plant Methods · doi:10.1186/s13007-024-01157-8 · Cited by 10 · see citing works
Tian, Y., Wang, H., Pan, T., Hu, X.-N., Ding, J., Chen, Y., Li, J. X., Chen, H., & Luo, T. (2024) · Journal of Proteomics · doi:10.1016/j.jprot.2024.105213 · Cited by 10 · see citing works
Histone variants and sensing of chromatin functional states
Govin, J., & Khochbin, S. (2013) · Nucleus · doi:10.4161/nucl.27088 · Cited by 10 · see citing works
Self-citationMetaboloepigenetics: The Emerging Network in Stem Cell Homeostasis Regulation
Avitabile, D., Magenta, A., Lauri, A., Gambini, E., Spaltro, G., & Vinci, M. C. (2016) · Current Stem Cell Research & Therapy · doi:10.2174/1574888x11666151203223839 · Cited by 10 · see citing works
Chemical Biology Approaches to Identify and Profile Interactors of Chromatin Modifications
Nickel, G. A., & Diehl, K. L. (2022) · ACS Chemical Biology · doi:10.1021/acschembio.1c00794 · Cited by 9 · see citing works
Live‐Cell Imaging of DNA Methylation Based on Synthetic‐Molecule/Protein Hybrid Probe
Kumar, N., Hori, Y., & Kikuchi, K. (2018) · The Chemical Record · doi:10.1002/tcr.201800039 · Cited by 9 · see citing works
The Brucella Effector Protein BspF Crotonylates TRIM38 to Inhibit NF-κB and MAPK Signaling Pathway
Zhang, H., Xing, Y., Zhu, J., Wu, S., Gao, J., Wang, Y., Yu, Z., Li, A., Li, Y., Chen, X., et al. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26083573 · Cited by 8 · see citing works
Protein crotonylation: Basic research and clinical diseases
Li, D., Lin, L., Xu, F., Feng, T., Tao, Y., Miao, H., & Yang, F. (2024) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2024.101694 · Cited by 8 · see citing works
Zhou, C., Zeng, H., Xiao, X., Wang, L., Jia, L., Shi, Y., Zhang, M., Fang, C., Zeng, Y., Wu, T., et al. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.129149 · Cited by 7 · see citing works
Epigenetics and its Role in Male Infertility
Tvrdá, E., Gosálvez, J., & Agarwal, A. K. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-800872-0.00036-6 · Cited by 7 · see citing works
Histone Modifications in Cardiovascular Disease: Mechanisms and Therapeutic Opportunities
Zheng, Y., Gao, Y., Guo, M., Wang, L., Zheng, X., Liao, Y., Li, Y., Zhu, J.-P., & Wei, J. (2026) · MedComm · doi:10.1002/mco2.70765 · Cited by 6 · see citing works
Cracking Lysine Crotonylation (Kcr): Enlightening a Promising Post‐Translational Modification
Westerveld, M., Besermenji, K., Aidukas, D., Ostrovitsa, N., & Petracca, R. (2024) · ChemBioChem · doi:10.1002/cbic.202400639 · Cited by 6 · see citing works
Li, W., Yan, W., Hao, F., Hao, L., & Liu, D. (2022) · Animals · doi:10.3390/ani12202848 · Cited by 5 · see citing works
Proteomic Analysis of Histone Crotonylation Suggests Diverse Functions in Myzus persicae
Xu, M., Xie, Y., Li, Y., Shen, L., Huang, K., Lin, Z., Li, B., Xia, C., Zhang, X., Chi, Y., et al. (2021) · ACS Omega · doi:10.1021/acsomega.1c01194 · Cited by 5 · see citing works
Histone-mediated transgenerational epigenetics
Cavalieri, V., & Spinelli, G. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-816363-4.00008-0 · Cited by 4 · see citing works
Reading and Interpreting the Histone Acylation Code
Soffers, J. H., Li, X., Abmayr, S. M., & Workman, J. L. (2016) · Genomics Proteomics & Bioinformatics · doi:10.1016/j.gpb.2016.12.001 · Cited by 4 · see citing works
Bi, J., Guo, Q., Zhou, Z., Huang, X., Qin, L., Tao, X., Ye, T., Chen, L., Li, G., Wang, Z., et al. (2022) · Microbiological Research · doi:10.1016/j.micres.2022.127209 · Cited by 4 · see citing works
Protein lysine acetylation regulates oral microorganisms
Yang, Y., He, H., Liu, B., Li, Z., Sun, J., Zhao, Z., & Yang, Y. (2025) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2025.1594947 · Cited by 2 · see citing works
Wang, J., Luo, Z., Geng, A., Xu, J., Meng, Y., Yan, S., Wei, L., Zhang, Z., Zhang, Q., Zou, Q., et al. (2025) · IEEE Transactions on Computational Biology and Bioinformatics · doi:10.1109/tcbbio.2025.3643930 · Cited by 2 · see citing works
- Authors
- Montellier, E., Rousseaux, S., Zhao, Y., & Khochbin, S.
- Affiliations
- Inserm (FR)
- Chinese Academy of Sciences (CN)
- Corresponding author
- Khochbin, Saadi
- Venue
- BioEssays
- Publisher
- Wiley
- Published
- 2011-12-15
- Volume
- 34
- Issue
- 3
- Pages
- 187-193
- ISSN
- 0265-9247 (ISSN-L)
- 1521-1878
- OpenAlex
- W2107882638
- Cited by
- 116
- References
- 46
- Citations by year
- 2026: 1 · 2025: 8 · 2024: 7 · 2023: 6 · 2022: 7 · 2021: 13 · 2020: 10 · 2019: 5 · 2018: 11 · 2017: 7 · 2016: 14 · 2015: 6 · 2014: 6 · 2013: 10 · 2012: 5
- FWCI
- 1.04
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- BioEssays (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Agence Nationale de la Recherche
- Institut National Du Cancer
- Topics
- Health Sciences › Medicine › Reproductive Medicine › Sperm and Testicular Function
- 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
- Keywords
- histone crotonylation, male germ cells, haploid cells, sex chromosome inactivation, spermatogenesis, autosomal genes, transcriptional repression
- MeSH terms
- Animals, Haploidy, Histone Deacetylases, Histones, Male, Mammals, Meiosis, Sex Chromosomes, Spermatocytes, Spermatogenesis, Testis, Transcriptional Activation, Gene Expression, Chromatin Assembly and Disassembly, Genes, X-Linked, Genes, Y-Linked
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