Structure and dynamic properties of nucleosome core particles

被引：53

作者：

Chakravarthy, S ^{[1
]}

Park, YJ ^{[1
]}

Chodaparambil, J ^{[1
]}

Edayathumangalam, RS ^{[1
]}

Luger, K ^{[1
]}

机构：

[1] Colorado State Univ, Dept Biochem & Mol Biol, Ft Collins, CO 80523 USA

来源：

FEBS LETTERS | 2005年 / 579卷 / 04期

关键词：

histone; chromatin; nucleosome; historic variant; sliding; crystal structure;

D O I：

10.1016/j.febslet.2004.11.030

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

It is now widely recognized that the packaging of genomic DNA, together with core histones, linker histones, and other functional proteins into chromatin profoundly influences nuclear processes such as transcription, replication, DNA repair, and recombination. Whereas earlier structural studies portrayed nucleosomes (the basic repeating unit of chromatin) as monolithic and static macromolecular assemblies, we now know that they are highly dynamic and capable of extensive crosstalk with the cellular machinery. Histone variants have evolved to locally after chromatin structure, whereas histone chaperones and other cellular factors promote histone exchange and chromatin fluidity. Both of these phenomena likely facilitate interconversion between different chromatin states that show varying degrees of transcriptional activity. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：895 / 898

页数：4

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