Contribution of histone N-terminal tails to the structure and stability of nucleosomes.
Contribution of histone N-terminal tails to the structure and stability of nucleosomes.
复制标题
组蛋白N末端尾巴对核小体的结构和稳定性的贡献。
DOI：
10.1016/j.fob.2013.08.007
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发表时间：
2013
期刊：
影响因子：
2.6
通讯作者：
Kurumizaka H
中科院分区：
文献类型：
--
作者：
Iwasaki W;Miya Y;Horikoshi N;Osakabe A;Taguchi H;Tachiwana H;Shibata T;Kagawa W;Kurumizaka H
组蛋白是核小体的蛋白质成分，核小体构成真核染色质的基本结构。组蛋白H2A、H2B、H3和H4由“组蛋白折叠”和“组蛋白尾部”两个共同区域组成。许多努力都集中在组蛋白尾部的翻译后修饰调节高阶染色质结构的机制上。另一方面，以往的生化研究表明，组蛋白尾部也会影响核小体核心颗粒本身的结构和稳定性。然而，每个组蛋白尾部的确切作用尚不清楚。在本研究中，我们确定了四种突变核小体的晶体结构，其中四种组蛋白H2A， H2B， H3或H4中的一种缺少n端尾部。我们发现H2B或H3 n端尾部的缺失会影响组蛋白与dna的相互作用，并显著降低核小体的稳定性。这些发现为理解组蛋白尾部在调节染色质结构中的复杂作用提供了重要信息。测定了四个n端无尾核小体的晶体结构。H2B n端尾缺失影响核小体中组蛋白- dna相互作用。H3 n端尾缺失影响核小体中组蛋白- dna相互作用。H2B或H3 n端缺失降低了核小体的稳定性。
Histones are the protein components of the nucleosome, which forms the basic architecture of eukaryotic chromatin. Histones H2A, H2B, H3, and H4 are composed of two common regions, the “histone fold” and the “histone tail”. Many efforts have been focused on the mechanisms by which the post-translational modifications of histone tails regulate the higher-order chromatin architecture. On the other hand, previous biochemical studies have suggested that histone tails also affect the structure and stability of the nucleosome core particle itself. However, the precise contributions of each histone tail are unclear. In the present study, we determined the crystal structures of four mutant nucleosomes, in which one of the four histones, H2A, H2B, H3, or H4, lacked the N-terminal tail. We found that the deletion of the H2B or H3 N-terminal tail affected histone–DNA interactions and substantially decreased nucleosome stability. These findings provide important information for understanding the complex roles of histone tails in regulating chromatin structure. The crystal structures of four N-terminal tail-less nucleosomes have been determined. H2B N-terminal tail deletion affected histone–DNA interactions in nucleosomes. H3 N-terminal tail deletion affected histone–DNA interactions in nucleosomes. H2B or H3 N-terminal deletion decreased the nucleosome stability.
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影响因子：
2.9
作者：
Bertin, A;Leforestier, A;Livolant, F
通讯作者：
Livolant, F
DOI：
10.1107/s0907444904019158
发表时间：
2004-12-01
影响因子：
2.2
作者：
Emsley, P;Cowtan, K
通讯作者：
Cowtan, K
DOI：
10.1073/pnas.121171498
发表时间：
2001-06-05
影响因子：
11.1
作者：
Angelov, D;Vitolo, JM;Hayes, JJ
通讯作者：
Hayes, JJ
影响因子：
11.4
作者：
de la Barre, AE;Angelov, D;Dimitrov, S
通讯作者：
Dimitrov, S
DOI：
10.1107/s0907444998003254
发表时间：
1998-09-01
期刊：
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
影响因子：
--
作者：
Brunger, AT;Adams, PD;Warren, GL
通讯作者：
Warren, GL