染色质
组蛋白
表观遗传学
核小体
组蛋白密码
生物
组蛋白修饰酶
染色质重塑
组蛋白H2A
遗传学
细胞生物学
组蛋白H1
DNA
计算生物学
基因
作者
Juan Ausió,D. Wade Abbott
出处
期刊:Biochemistry
[American Chemical Society]
日期:2002-04-20
卷期号:41 (19): 5945-5949
被引量:90
摘要
For many years, histones were considered to be passive structural components of eukaryotic chromatin. Experimental evidence that has accumulated during the past few years indicates that in addition to their structural role, histones play a very important functional role and that they can operate as epigenetic markers. This notion has rekindled the interest in histone variants and their participation in the processes of chromatin activation and inactivation. Recent papers have focused their attention on histone H2A variants. The variants of this overlooked histone participate in many biological processes ranging from transcriptional activation to DNA repair, meiosis, and apoptosis. A nucleosome containing at least one of these variants has been crystallized and biophysically characterized in solution. From all these results, a new concept has started to emerge, which supports the notion that the functional roles of H2A variants are exerted through alterations in chromatin stability and folding that result from the structural variation at the carboxyl-terminal end of this histone.
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