Rad52 associates with RPA and functions with Rad55 and Rad57 to assemble meiotic recombination complexes
Rad52 associates with RPA and functions with Rad55 and Rad57 to assemble meiotic recombination complexes
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DOI：
10.1101/gad.12.14.2208
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发表时间：
1998-07-15
影响因子：
10.5
通讯作者：
Bishop, DK
中科院分区：
文献类型：
--
作者：
Gasior, SL;Wong, AK;Bishop, DK
我们发现酿酒酵母重组蛋白Rad52和单链DNA结合蛋白RPA在减数分裂重组过程中组装成在细胞学上可检测的亚核复合物（焦点）。免疫染色显示Rad52和RPA广泛共定位，以及Rad52与链交换蛋白Rad51有限的分子共定位。Rad52和RPA焦点不同于由Rad51及其减数分裂特异性相关蛋白Dmc1形成的焦点，因为它们在复制期间的减数分裂过程中也能被检测到。此外，在有丝分裂S期也能观察到RPA焦点。双链断裂（DSBs）促进RPA、Rad52和Rad51焦点的形成。Back Spoil（一种DSB形成所必需的蛋白）的突变体在焦点形成方面存在缺陷，并且这种缺陷可被电离辐射以剂量依赖的方式抑制。DSBs不足以使Rad51焦点出现；Rad52、Rad55和Rad57也是必需的，这支持了一种模型，即这三种蛋白通过促进链交换复合物的组装来促进减数分裂重组。
We show that the Saccharomyces cerevisiae recombination protein Rad52 and the single-strand DNA-binding protein RPA assemble into cytologically detectable subnuclear complexes (foci) during meiotic recombination. Immunostaining shows extensive colocalization of Rad52 and RPA and mole limited colocalization of Rad52 with the strand exchange protein Rad51. Rad52 and RPA foci are distinct from those formed by Rad51, and its meiosis-specific relative Dmc1, in that they are also detected in meiosis during replication. In addition, RPA foci are observed during mitotic S phase. Double-strand breaks (DSBs) promote formation of RPA, Rad52, and Rad51 foci. Mutants that Back Spoil, a protein required for DSB formation, are defective in focus formation, and this defect is suppressed by ionizing radiation in a dose-dependent manner. DSBs are not sufficient for the appearance of Rac51 foci; Rad52, Rad55, and Rad57 are also required supporting a model in which these three proteins promote meiotic recombination by promoting the assembly of strand exchange complexes.