The N-terminal tail of histone H2A binds to two distinct sites within the nucleosome core

Kyu-Min Lee; Jeffrey J. Hayes

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The N-terminal tail of histone H2A binds to two distinct sites within the nucleosome core

机译：组蛋白H2A的N末端尾巴与核小体核心内的两个不同位点结合

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Each of the core histone proteins within the nucleosome has a central "structured" domain that comprises the spool onto which the DNA superhelix is wrapped and an N-terminal "tail" domain in which the structure and molec- ular interactions have not been rigorously defined. Recent studies have shown that the N-terminal domains of core histones probably contact both DNA and proteins within the nucleus and that these interactions play key roles in the regulation of nuclear processes (such as transcription and replication) and are critical in the formation of the chromatin fiber. An understanding of these complex mechanisms awaits identification of the DNA or protein sites within chromatin contacted by the tail domains.

机译：核小体中的每个核心组蛋白都具有一个中央“结构化”结构域，该结构域包括缠绕有DNA超螺旋的线轴和一个N末端“尾部”结构域，在该结构域中，结构和分子的相互作用尚未得到严格定义。最近的研究表明，核心组蛋白的N末端结构域可能会接触细胞核内的DNA和蛋白质，并且这些相互作用在调节核过程（例如转录和复制）中起着关键作用，并且对形成核糖核酸至关重要。染色质纤维。对这些复杂机制的理解有待鉴定与尾结构域接触的染色质中的DNA或蛋白质位点。

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《Proceedings of the National Academy of Sciences of the United States of America》 |1997年第17期|p.8959-8964|共6页
作者
Kyu-Min Lee; Jeffrey J. Hayes;
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收录信息美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
原文格式 PDF
正文语种 eng
中图分类自然科学总论;
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1. The Core Histone N-Terminal Tail Domains Negatively Regulate Binding of Transcription Factor IIIA to a Nucleosome Containing a 5S RNA Gene via a Novel Mechanism [J] . Zungyoon Yang, Chunyang Zheng, Christophe Thiriet, Molecular and Cellular Biology . 2005,第1期

机译：核心组蛋白N末端尾域通过一种新机制，负调控转录因子IIIA与包含5S RNA基因的核小体的结合。
2. Distinct Roles of Histone H3 and H2A Tails in Nucleosome Stability [J] . Zhenhai Li, Hidetoshi Kono Scientific reports. . 2016,第1期

机译：组蛋白H3和H2A尾巴在核小体稳定性中的不同作用
3. Role of Direct Interactions between the Histone H4 Tail and the H2A Core in Long Range Nucleosome Contacts [J] . Divya Sinha, Michael Shogren-Knaak The Journal of biological chemistry . 2010,第22期

机译：组蛋白H4尾部之间的直接相互作用的作用和长距离核小组联系的H2A核心
4. Recognition of the N-Terminal Histone H2A and H3 Peptides by Peptidylarginine Deiminase V [C] . Yuji Hidaka, Mayumi Watase, Hironori Matsubayashi International Peptide Symposium . 2009

机译：通过Peptidyl族氨基酶V识别N-末端组蛋白H2A和H3肽
5. Characterizing ΔNp63α Binding Sites Based on Nucleosome Organization and Histone Modifications [D] . Tabrejee, Shamira. 2020

机译：基于核小体组织和组蛋白修改的Δnp63α结合位点
6. The N-terminal tail of histone H2A binds to two distinct sites within the nucleosome core [O] . Kyu-Min Lee, Jeffrey J. Hayes 1997

机译：组蛋白H2A的N末端尾巴与核小体核心中的两个不同位点结合
7. The Core Histone N-Terminal Tail Domains Negatively Regulate Binding of Transcription Factor IIIA to a Nucleosome Containing a 5S RNA Gene via a Novel Mechanism [O] . Yang, Zungyoon, Zheng, Chunyang, Thiriet, Christophe, 2005

机译：核心组蛋白N末端尾域通过一种新的机制负调控转录因子IIIA与包含5S RNA基因的核小体的结合。
8. Chromatin Regulation of Estrogen-Mediated Transcription in Breast Cancer: Rules for Binding Sites in Nucleosomes and Modified Histones that Enhance ER Binding [R] . Chrivia, J. C. 2005

机译：染色质调节乳腺癌中雌激素介导的转录：核小体中结合位点的规则和增强ER结合的修饰组蛋白

The N-terminal tail of histone H2A binds to two distinct sites within the nucleosome core

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