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双 Holliday junction 溶解的分子机制。

Molecular mechanism of double Holliday junction dissolution.

机构信息

Clare Hall laboratories, Cancer Research U.K. London Research Institute, London EN6 3LD, UK.

出版信息

Cell Biosci. 2014 Jul 9;4:36. doi: 10.1186/2045-3701-4-36. eCollection 2014.

Abstract

Processing of homologous recombination intermediates is tightly coordinated to ensure that chromosomal integrity is maintained and tumorigenesis avoided. Decatenation of double Holliday junctions, for example, is catalysed by two enzymes that work in tight coordination and belong to the same 'dissolvasome' complex. Within the dissolvasome, the RecQ-like BLM helicase provides the translocase function for Holliday junction migration, while the topoisomerase III alpha-RMI1 subcomplex works as a proficient DNA decatenase, together resulting in double-Holliday-junction unlinking. Here, we review the available architectural and biochemical knowledge on the dissolvasome machinery, with a focus on the structural interplay between its components.

摘要

同源重组中间体的处理需要紧密协调,以确保染色体的完整性得以维持,避免肿瘤发生。例如,双 Holliday 连接点的解连环由两种紧密协调的酶催化,它们属于同一个“解旋酶体”复合物。在解旋酶体中,RecQ 样 BLM 解旋酶提供 Holliday 连接点迁移的转位酶功能,而拓扑异构酶 III alpha-RMI1 亚基作为有效的 DNA 解连环酶,共同导致双 Holliday 连接点的解连环。在这里,我们综述了关于解旋酶体机制的现有结构和生化知识,重点介绍了其组成部分之间的结构相互作用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5c12/4109787/4b08434e2593/2045-3701-4-36-1.jpg

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