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人类RAD52蛋白的自我缔合。

Self-association of human RAD52 protein.

作者信息

Shen Z, Peterson S R, Comeaux J C, Zastrow D, Moyzis R K, Bradbury E M, Chen D J

机构信息

Life Sciences Division, Los Alamos National Laboratory, NM 87545, USA.

出版信息

Mutat Res. 1996 Oct 18;364(2):81-9. doi: 10.1016/0921-8777(96)00025-0.

Abstract

The yeast RAD52 protein is required for both homologous DNA recombination and repair of DNA double-strand breaks. RAD52 can bind to the yeast RAD51 protein, which shares a functional similarity with the bacterial RecA protein. The gene encoding the human homolog of the yeast RAD52 protein shares significant N-terminus amino acid homology with the yeast RAD52 protein. Using a yeast two hybrid system and purified GST-RAD52 fusion protein, we demonstrate that the human RAD52 protein self-associates both in vivo and in vitro. The region of RAD52 required for its self-interaction, mapped here as amino acid residues 65-165, has significant homology with the yeast RAD52 (52% identity, and 89% similarity), suggesting the importance of self-association for RAD52's function.

摘要

酵母RAD52蛋白对于同源DNA重组和DNA双链断裂的修复都是必需的。RAD52能与酵母RAD51蛋白结合,后者与细菌RecA蛋白具有功能相似性。编码酵母RAD52蛋白人类同源物的基因与酵母RAD52蛋白在N端氨基酸上有显著的同源性。利用酵母双杂交系统和纯化的GST-RAD52融合蛋白,我们证明人类RAD52蛋白在体内和体外都能自我缔合。RAD52自我相互作用所需的区域,定位为氨基酸残基65-165,与酵母RAD52有显著同源性(52%相同,89%相似),表明自我缔合对RAD52功能的重要性。

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