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从RuvA结构洞察同源重组机制。

Insights into the mechanisms of homologous recombination from the structure of RuvA.

作者信息

Rice D W, Rafferty J B, Artymiuk P J, Lloyd R G

机构信息

Krebs Institute, Department of Molecular Biology and Biotechnology, University of Sheffield, UK.

出版信息

Curr Opin Struct Biol. 1997 Dec;7(6):798-803. doi: 10.1016/s0959-440x(97)80149-2.

DOI:10.1016/s0959-440x(97)80149-2
PMID:9434898
Abstract

The recent structure determination of RuvA has provided the first insights into the structural basis for its interaction with Holliday junction DNA. Multiple copies of a helix-hairpin-helix motif which line the four grooves between the monomers in the tetrameric structure are thought to be involved in the interaction of the protein with its DNA target. This suggests that the four arms of the junction are held by RuvA in a fourfold symmetric arrangement and has fuelled ideas on the way in which components of the Ruv complex combine to catalyse the process of homologous recombination.

摘要

最近对RuvA的结构测定首次揭示了其与霍利迪连接体DNA相互作用的结构基础。在四聚体结构中,排列在单体之间四条沟中的多个螺旋-发夹-螺旋基序拷贝被认为参与了该蛋白质与其DNA靶点的相互作用。这表明连接体的四条臂被RuvA以四重对称排列固定住,这引发了人们对Ruv复合体各组分如何结合以催化同源重组过程的思考。

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Insights into the mechanisms of homologous recombination from the structure of RuvA.从RuvA结构洞察同源重组机制。
Curr Opin Struct Biol. 1997 Dec;7(6):798-803. doi: 10.1016/s0959-440x(97)80149-2.
2
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Structural similarities between Escherichia coli RuvA protein and other DNA-binding proteins and a mutational analysis of its binding to the holliday junction.大肠杆菌RuvA蛋白与其他DNA结合蛋白之间的结构相似性及其与霍利迪连接体结合的突变分析。
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Processing the holliday junction in homologous recombination.处理同源重组中的霍利迪连接体。
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The acidic pin of RuvA modulates Holliday junction binding and processing by the RuvABC resolvasome.RuvA的酸性结构域通过RuvABC解离酶体调节霍利迪连接体的结合与加工。
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Analysis of conserved basic residues associated with DNA binding (Arg69) and catalysis (Lys76) by the RusA holliday junction resolvase.RusA霍利迪连接体解离酶对与DNA结合(精氨酸69)和催化作用(赖氨酸76)相关的保守碱性残基的分析。
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