Quantitative proteomic analysis of histone modifications.

Quantitative proteomic analysis of histone modifications.
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DOI:
10.1021/cr500491u
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发表时间:
2015-03-25
期刊:
影响因子:
62.1
通讯作者:
Zhao Y
Zhao Y
中科院分区:
化学1区
文献类型:
--
作者:
Huang H;Lin S;Garcia BA;Zhao Y

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Several mechanisms have been proposed for histone marks to exert their functions, including altering the physical properties of nucleosomes by neutralization of charge via acetylation, resulting in increasing nucleosome mobility and modulation of the higher order chromatin structure. 24b In addition, histone marks often act through the recruitment of downstream molecules, referred to as “readers” or “effectors”, which specifically recognize a particular modification in the context of the histone molecule or nucleosomes. 1c, 291 Here, a few terms for the relevant proteins are defined. We would like to define a protein “reader” of a histone marks as a protein that directly interacts and recognizes a specific histone mark in a particular sequence context; a protein “binder” as a protein that either directly or indirectly associates with a histone, in a modification-dependent or-independent manner; and a “effector” as a protein that binds specifically to a posttranslational modified histone substrate, and this binding event recruits other activities contained within the same polypeptide or complex. Thus,“effectors” translate histone marks into biological output. A “reader” is a direct “binder” of a histone mark.