组蛋白结构与核小体稳定性。
Histone structure and nucleosome stability.
作者信息
Mariño-Ramírez Leonardo, Kann Maricel G, Shoemaker Benjamin A, Landsman David
机构信息
Computational Biology Branch, National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA.
出版信息
Expert Rev Proteomics. 2005 Oct;2(5):719-29. doi: 10.1586/14789450.2.5.719.
Abstract
Histone proteins play essential structural and functional roles in the transition between active and inactive chromatin states. Although histones have a high degree of conservation due to constraints to maintain the overall structure of the nucleosomal octameric core, variants have evolved to assume diverse roles in gene regulation and epigenetic silencing. Histone variants, post-translational modifications and interactions with chromatin remodeling complexes influence DNA replication, transcription, repair and recombination. The authors review recent findings on the structure of chromatin that confirm previous interparticle interactions observed in crystal structures.
摘要
组蛋白在活性染色质状态与非活性染色质状态之间的转变过程中发挥着至关重要的结构和功能作用。尽管由于维持核小体八聚体核心整体结构的限制，组蛋白具有高度保守性，但变体已经进化出来，在基因调控和表观遗传沉默中发挥多种作用。组蛋白变体、翻译后修饰以及与染色质重塑复合物的相互作用会影响DNA复制、转录、修复和重组。作者回顾了关于染色质结构的最新发现，这些发现证实了先前在晶体结构中观察到的颗粒间相互作用。
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本文引用的文献
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