Structure of a RSC-nucleosome complex and insights into chromatin remodeling.

Structure of a RSC-nucleosome complex and insights into chromatin remodeling.
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DOI:
10.1038/nsmb.1524
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发表时间:
2008-12
影响因子:
16.8
通讯作者:
--
中科院分区:
生物学1区
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--
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atp依赖性染色质重塑复合体,如RSC,可以重新定位、排出或重组核小体。冷冻电镜(cro - em)测定的RSC -核小体复合物结构显示核小体结合在中央RSC腔内。RSC与组蛋白和DNA的广泛相互作用似乎破坏了核小体的稳定,并导致其结构的整体不依赖于atp的重排。核小体DNA似乎是无序的,并且在重塑所需的情况下,很大程度上可以自由地凸出到溶液中,但RSC -核小体复合物的结构表明,RSC不太可能将其结合的核小体的八聚体移走。考虑到RSC -核小体的结构和已发表的生化信息表明,RSC依赖atp的DNA易位可能导致组蛋白八聚体从邻近的核小体中移除。
ATP-dependent chromatin-remodeling complexes, such as RSC, can reposition, evict or restructure nucleosomes. A structure of a RSC–nucleosome complex with a nucleosome determined by cryo-EM shows the nucleosome bound in a central RSC cavity. Extensive interaction of RSC with histones and DNA seems to destabilize the nucleosome and lead to an overall ATP-independent rearrangement of its structure. Nucleosomal DNA appears disordered and largely free to bulge out into solution as required for remodeling, but the structure of the RSC–nucleosome complex indicates that RSC is unlikely to displace the octamer from the nucleosome to which it is bound. Consideration of the RSC–nucleosome structure and published biochemical information suggests that ATP-dependent DNA translocation by RSC may result in the eviction of histone octamers from adjacent nucleosomes.
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