Ogawa T, Yu X, Shinohara A, Egelman E H
Department of Biology, Osaka University, Japan.
Science. 1993 Mar 26;259(5103):1896-9. doi: 10.1126/science.8456314.
The RAD51 protein functions in the processes of DNA repair and in mitotic and meiotic genetic recombination in the yeast Saccharomyces cerevisiae. The protein has adenosine triphosphate-dependent DNA binding activities similar to those of the Escherichia coli RecA protein, and the two proteins have 30 percent sequence homology. RAD51 polymerized on double-stranded DNA to form a helical filament nearly identical in low-resolution, three-dimensional structure to that formed by RecA. Like RecA, RAD51 also appears to force DNA into a conformation of approximately a 5.1-angstrom rise per base pair and 18.6 base pairs per turn. As in other protein families, its structural conservation appears to be stronger than its sequence conservation. Both the structure of the protein polymer formed by RecA and the DNA conformation induced by RecA appear to be general properties of a class of recombination proteins found in prokaryotes as well as eukaryotes.
RAD51蛋白在酿酒酵母的DNA修复过程以及有丝分裂和减数分裂遗传重组过程中发挥作用。该蛋白具有与大肠杆菌RecA蛋白相似的三磷酸腺苷依赖性DNA结合活性，且这两种蛋白具有30%的序列同源性。RAD51在双链DNA上聚合形成螺旋丝，其低分辨率三维结构与RecA形成的结构几乎相同。与RecA一样，RAD51似乎也迫使DNA形成一种每碱基对上升约5.1埃、每圈18.6个碱基对的构象。与其他蛋白质家族一样，其结构保守性似乎比序列保守性更强。RecA形成的蛋白质聚合物结构以及RecA诱导的DNA构象似乎是原核生物和真核生物中一类重组蛋白的普遍特性。
