气候变化领域集成服务门户(CCPortal): Histone H3Q5 serotonylation stabilizes H3K4 methylation and potentiates its readout

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DOI	10.1073/pnas.2016742118
	Histone H3Q5 serotonylation stabilizes H3K4 methylation and potentiates its readout
	Zhao S.; Chuh K.N.; Zhang B.; Dul B.E.; Thompson R.E.; Farrelly L.A.; Liu X.; Xu N.; Xue Y.; Roeder R.G.; Maze I.; Muir T.W.; Li H.
发表日期	2021
ISSN	00278424
卷号	118 期号:6
英文摘要	Serotonylation of glutamine 5 on histone H3 (H3Q5ser) was recently identified as a permissive posttranslational modification that coexists with adjacent lysine 4 trimethylation (H3K4me3). While the resulting dual modification, H3K4me3Q5ser, is enriched at regions of active gene expression in serotonergic neurons, the molecular outcome underlying H3K4me3-H3Q5ser crosstalk remains largely unexplored. Herein, we examine the impact of H3Q5ser on the readers, writers, and erasers of H3K4me3. All tested H3K4me3 readers retain binding to the H3K4me3Q5ser dual modification. Of note, the PHD finger of TAF3 favors H3K4me3Q5ser, and this binding preference is dependent on the Q5ser modification regardless of H3K4 methylation states. While the activity of the H3K4 methyltransferase, MLL1, is unaffected by H3Q5ser, the corresponding H3K4me3/2 erasers, KDM5B/C and LSD1, are profoundly inhibited by the presence of the mark. Collectively, this work suggests that adjacent H3Q5ser potentiates H3K4me3 function by either stabilizing H3K4me3 from dynamic turnover or enhancing its physical readout by downstream effectors, thereby potentially providing a mechanism for fine-tuning critical gene expression programs. © 2021 National Academy of Sciences. All rights reserved.
英文关键词	Designer chromatin; H3K4me3; H3Q5 serotonylation; Histone modification; Modification crosstalk
语种	英语
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/180709
作者单位	Ministry of Education Key Laboratory of Protein Sciences, Beijing Advanced Innovation Center for Structural Biology, Beijing Frontier Research Center for Biological Structure, Department of Basic Medical Sciences, School of Medicine, Tsinghua University, Beijing, 100084, China; Department of Chemistry, Princeton University, Princeton, NJ 08540, United States; Nash Family Department of Neuroscience, Friedman Brain Institute, Icahn School of Medicine at Mount Sinai, New York, NY 10029, United States; Department of Pharmacological Sciences, Icahn School of Medicine at Mount Sinai, New York, NY 10029, United States; National Protein Science Technology Center, School of Life Sciences, Tsinghua University, Beijing, 100084, China; Laboratory of Biochemistry and Molecular Biology, Rockefeller University, New York, NY 10065, United States; Tsinghua-Peking Center for Life Sciences, Tsinghua University, Beijing, 100084, China
推荐引用方式 GB/T 7714	Zhao S.,Chuh K.N.,Zhang B.,et al. Histone H3Q5 serotonylation stabilizes H3K4 methylation and potentiates its readout[J],2021,118(6).
APA	Zhao S..,Chuh K.N..,Zhang B..,Dul B.E..,Thompson R.E..,...&Li H..(2021).Histone H3Q5 serotonylation stabilizes H3K4 methylation and potentiates its readout.Proceedings of the National Academy of Sciences of the United States of America,118(6).
MLA	Zhao S.,et al."Histone H3Q5 serotonylation stabilizes H3K4 methylation and potentiates its readout".Proceedings of the National Academy of Sciences of the United States of America 118.6(2021).