Acetyl-methyllysine marks chromatin at active transcription start sites

乙酰化 染色质 组蛋白 赖氨酸 甲基化 生物化学 组蛋白修饰酶 染色质重塑 溴尿嘧啶 生物 蛋白质甲基化 化学 组蛋白甲基转移酶 组蛋白密码 细胞生物学 核小体 基因 甲基转移酶 氨基酸
作者
William J. Lu-Culligan,Leah J. Connor,Yixuan Xie,Babatunde Ekundayo,Brendan T Rose,Martin Machyna,Andreas P. Pintado-Urbanc,Joshua T. Zimmer,Isaac W. Vock,Natarajan V. Bhanu,Megan C. King,Benjamin A. Garcia,Franziska Bleichert,Matthew D. Simon
出处
期刊:Nature [Springer Nature]
卷期号:622 (7981): 173-179 被引量:12
标识
DOI:10.1038/s41586-023-06565-9
摘要

Lysine residues in histones and other proteins can be modified by post-translational modifications that encode regulatory information1. Lysine acetylation and methylation are especially important for regulating chromatin and gene expression2–4. Pathways involving these post-translational modifications are targets for clinically approved therapeutics to treat human diseases. Lysine methylation and acetylation are generally assumed to be mutually exclusive at the same residue. Here we report cellular lysine residues that are both methylated and acetylated on the same side chain to form Nε-acetyl-Nε-methyllysine (Kacme). We show that Kacme is found on histone H4 (H4Kacme) across a range of species and across mammalian tissues. Kacme is associated with marks of active chromatin, increased transcriptional initiation and is regulated in response to biological signals. H4Kacme can be installed by enzymatic acetylation of monomethyllysine peptides and is resistant to deacetylation by some HDACs in vitro. Kacme can be bound by chromatin proteins that recognize modified lysine residues, as we demonstrate with the crystal structure of acetyllysine-binding protein BRD2 bound to a histone H4Kacme peptide. These results establish Kacme as a cellular post-translational modification with the potential to encode information distinct from methylation and acetylation alone and demonstrate that Kacme has all the hallmarks of a post-translational modification with fundamental importance to chromatin biology. Cellular lysine residues can be both methylated and acetylated on the same sidechain to form Nε-acetyl-Nε-methyllysine (Kacme), which is found on histone H4 across a range of species and across mammalian tissues and is associated with active chromatin.
最长约 10秒,即可获得该文献文件

科研通智能强力驱动
Strongly Powered by AbleSci AI
更新
大幅提高文件上传限制,最高150M (2024-4-1)

科研通是完全免费的文献互助平台,具备全网最快的应助速度,最高的求助完成率。 对每一个文献求助,科研通都将尽心尽力,给求助人一个满意的交代。
实时播报
刚刚
小杨发布了新的文献求助10
1秒前
隐形曼青应助luxun采纳,获得10
2秒前
从一发布了新的文献求助10
2秒前
hl268完成签到,获得积分20
3秒前
古藤完成签到,获得积分10
3秒前
3秒前
杳鸢应助韦老虎采纳,获得10
4秒前
等待的音响完成签到,获得积分10
5秒前
董小帅完成签到,获得积分10
6秒前
6秒前
7秒前
魏亚情完成签到,获得积分10
7秒前
8秒前
文献下载中完成签到,获得积分10
8秒前
8秒前
bobo发布了新的文献求助10
9秒前
龙骑士25发布了新的文献求助30
10秒前
11秒前
11秒前
zjh关闭了zjh文献求助
12秒前
慕青应助开心采纳,获得10
13秒前
佩奇发布了新的文献求助10
13秒前
吴彦祖发布了新的文献求助10
13秒前
男爵发布了新的文献求助10
14秒前
14秒前
ruiii发布了新的文献求助10
14秒前
DTP完成签到,获得积分10
15秒前
lalala应助梨涡采纳,获得20
15秒前
在水一方应助bobo采纳,获得10
15秒前
16秒前
讨厌下雨发布了新的文献求助10
16秒前
16秒前
Aura吴发布了新的文献求助10
17秒前
香蕉觅云应助孤独代亦采纳,获得10
17秒前
SciGPT应助汤姆采纳,获得10
18秒前
所所应助嘎嘎嘎嘎采纳,获得10
18秒前
ice7应助王熊猫采纳,获得10
18秒前
我是老大应助欢喜秋寒采纳,获得10
18秒前
jingwen发布了新的文献求助10
18秒前
高分求助中
The late Devonian Standard Conodont Zonation 2000
Nickel superalloy market size, share, growth, trends, and forecast 2023-2030 2000
The Lali Section: An Excellent Reference Section for Upper - Devonian in South China 1500
Very-high-order BVD Schemes Using β-variable THINC Method 870
Mantiden: Faszinierende Lauerjäger Faszinierende Lauerjäger 800
PraxisRatgeber: Mantiden: Faszinierende Lauerjäger 800
Development of general formulas for bolted flanges, by E.O. Waters [and others] 500
热门求助领域 (近24小时)
化学 医学 生物 材料科学 工程类 有机化学 生物化学 物理 内科学 纳米技术 计算机科学 化学工程 复合材料 基因 遗传学 催化作用 物理化学 免疫学 量子力学 细胞生物学
热门帖子
关注 科研通微信公众号,转发送积分 3255241
求助须知:如何正确求助?哪些是违规求助? 2897655
关于积分的说明 8297443
捐赠科研通 2566693
什么是DOI,文献DOI怎么找? 1393842
科研通“疑难数据库(出版商)”最低求助积分说明 652658
邀请新用户注册赠送积分活动 630306