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由大肠杆菌RuvAB运动蛋白引导的霍利迪连接体通过核小体的迁移。

Migration of a Holliday junction through a nucleosome directed by the E. coli RuvAB motor protein.

作者信息

Grigoriev M, Hsieh P

机构信息

Genetics and Biochemistry Branch, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-1810, USA.

出版信息

Mol Cell. 1998 Sep;2(3):373-81. doi: 10.1016/s1097-2765(00)80281-6.

Abstract

Chromatin plays a critical role in regulating access to DNA by proteins that direct recombination and repair. The E. coli RuvAB protein complex promotes branch migration of the Holliday junction recombination intermediate. The ability of RuvAB to negotiate passage of the junction through nucleosomal DNA is examined. The model system involves the formation of a Holliday junction positioned upstream of a nucleosome. Unassisted, the junction is blocked by a histone octamer. In the presence of RuvAB and ATP, rapid branch migration through the nucleosome is observed. It results in disruption of the histone-DNA interactions leading to the removal of the octamer from the junction intermediate. These results suggest that eukaryotic DNA motor proteins analogous to RuvAB could function during recombination to promote branch migration through chromatin.

摘要

染色质在调控指导重组和修复的蛋白质对DNA的访问中起着关键作用。大肠杆菌RuvAB蛋白复合物促进霍利迪连接体重组中间体的分支迁移。研究了RuvAB使连接体穿过核小体DNA的能力。该模型系统涉及在核小体上游形成一个霍利迪连接体。在没有辅助的情况下,连接体被组蛋白八聚体阻断。在RuvAB和ATP存在的情况下,观察到连接体快速穿过核小体进行分支迁移。这导致组蛋白与DNA的相互作用被破坏,从而使八聚体从连接体中间体上移除。这些结果表明,类似于RuvAB的真核生物DNA运动蛋白可能在重组过程中发挥作用,以促进连接体穿过染色质进行分支迁移。

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