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首页> 外文期刊>Journal of Molecular Biology >Human Rad51 amino acid residues required for Rad52 binding.
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Human Rad51 amino acid residues required for Rad52 binding.

机译：Rad52结合所需的人类Rad51氨基酸残基。

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摘要

The Rad51 protein, a homologue of the bacterial RecA protein, is an essential factor for both meiotic and mitotic recombination. The N-terminal domain of the human Rad51 protein (HsRad51) directly interacts with DNA. Based on a yeast two-hybrid analysis, it has been reported that the N-terminal region of the Saccharomyces cerevisiae Rad51 protein binds Rad52;S. cerevisiae Rad51 and Rad52 both activate the homologous pairing and strand exchange reactions. Here, we show that the HsRad51 N-terminal region, which corresponds to the Rad52-binding region of ScRad51, does not exhibit strong binding to the human Rad52 protein (HsRad52). To investigate its function, the C-terminal region of HsRad51 was randomly mutagenized. Although this region includes the two segments corresponding to the putative DNA-binding sites of RecA, all seven of the mutants did not decrease, but instead slightly increased, the DNA binding. In contrast, we found that some of these HsRad51 mutations significantly decreased the HsRad52 binding. Therefore, we conclude that these amino acid residues are required for the HsRad51.HsRad52 binding. HsRad52, as well as S. cerevisiae Rad52, promoted homologous pairing between ssDNA and dsDNA, and higher homologous pairing activity was observed in the presence of both HsRad51 and HsRad52 than with either HsRad51 or HsRad52 alone. The HsRad51 F259V mutation, which strongly impaired the HsRad52 binding, decreased the homologous pairing in the presence of both HsRad51 and HsRad52, without affecting the homologous pairing by HsRad51 alone. This result suggests the importance of the HsRad51.HsRad52 interaction in homologous pairing. Copyright 1999 Academic Press.
机译：Rad51蛋白是细菌RecA蛋白的同源物，是减数分裂和有丝分裂重组的重要因素。人类Rad51蛋白（HsRad51）的N末端结构域与DNA直接相互作用。基于酵母的两杂交分析，已经报道了酿酒酵母Rad51蛋白的N末端区域结合了Rad52; S。酿酒酵母Rad51和Rad52均激活同源配对和链交换反应。在这里，我们显示HsRad51 N端区域，对应于ScRad51的Rad52结合区域，不表现出与人Rad52蛋白（HsRad52）的强结合。为了研究其功能，随机诱变了HsRad51的C端区域。尽管该区域包括对应于RecA假定的DNA结合位点的两个片段，但所有七个突变体的DNA结合率均未降低，但略有增加。相反，我们发现这些HsRad51突变中的一些显着降低了HsRad52的结合。因此，我们得出结论，这些氨基酸残基是HsRad51.HsRad52结合所必需的。 HsRad52和酿酒酵母Rad52促进ssDNA和dsDNA之间的同源配对，并且在同时存在HsRad51和HsRad52时观察到的同源配对活性高于单独使用HsRad51或HsRad52。 HsRad51 F259V突变严重削弱了HsRad52的结合，在同时存在HsRad51和HsRad52的情况下降低了同源配对，而不会影响仅由HsRad51进行的同源配对。该结果表明HsRad51.HsRad52相互作用在同源配对中的重要性。版权所有1999，学术出版社。

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