Valine 1532 of human BRC repeat 4 plays an important role in the interaction between BRCA2 and RAD51
Valine 1532 of human BRC repeat 4 plays an important role in the interaction between BRCA2 and RAD51
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DOI：
10.1016/j.febslet.2011.05.027
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发表时间：
2011-06-23
期刊：
影响因子：
3.5
通讯作者：
Morimatsu, Masami
中科院分区：
文献类型：
--
作者：
Ochiai, Kazuhiko;Yoshikawa, Yasunaga;Morimatsu, Masami
乳腺癌易感蛋白 BRCA2 对于重组 DNA 修复至关重要。 BRCA2 通过八个 BRC 重复基序特异性结合 RAD51，并将 RAD51 传递至双链 DNA 断裂处。在这项研究中，哺乳动物双杂交测定和竞争性 ELISA 表明，BRC 重复序列 4 (BRC4) 和 RAD51 之间的相互作用通过将单个 BRC4 氨基酸从缬氨酸替换为异亮氨酸 (V1532I) 得到加强。然而，与癌症相关的 V1532F 突变体与 RAD51 表现出非常弱的相互作用。本研究使用动物物种之间 BRC4 的比较分析，确定 V1532 是与 RAD51 相互作用的重要残基。 蛋白质相互作用的结构化摘要：cRAD51 通过两个杂交与 cRAD51 物理相互作用（查看相互作用）fBRC4 通过两个杂交与 cRAD51 物理相互作用（查看相互作用）cBRC4 通过两个杂交与 cRAD51 物理相互作用（查看相互作用）hBRC4 与 hBRC4 和hRAD51 通过竞争结合（查看相互作用 1、2）hBRC4 通过两个杂交与 cRAD51 发生物理相互作用（查看相互作用）hBRC4 通过酶联免疫吸附测定法与 hRAD51 结合（查看相互作用）(C) 2011 年欧洲生化协会联合会。由 Elsevier B.V. 出版。保留所有权利。
The breast cancer susceptibility protein BRCA2 is essential for recombinational DNA repair. BRCA2 specifically binds to RAD51 via eight BRC repeat motifs and delivers RAD51 to double-stranded DNA breaks. In this study, a mammalian two-hybrid assay and competitive ELISA showed that the interaction between BRC repeat 4 (BRC4) and RAD51 was strengthened by the substitution of a single BRC4 amino acid from valine to isoleucine (V1532I). However, the cancer-associated V1532F mutant exhibited very weak interaction with RAD51. This study used a comparative analysis of BRC4 between animal species to identify V1532 as an important residue that interacts with RAD51.Structured summary of protein interactions:cRAD51 physically interacts with cRAD51 by two hybrid (View interaction)fBRC4 physically interacts with cRAD51 by two hybrid (View interaction)cBRC4 physically interacts with cRAD51 by two hybrid (View interaction)hBRC4 physically interacts with hBRC4 and hRAD51 by competition binding (View Interaction 1, 2)hBRC4 physically interacts with cRAD51 by two hybrid (View interaction)hBRC4 binds to hRAD51 by enzyme linked immunosorbent assay (View interaction)(C) 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.