Crystal structure of the homologous-pairing domain from the human Rad52 recombinase in the undecameric form

被引:188
作者
Kagawa, W
Kurumizaka, H
Ishitani, R
Fukai, S
Nureki, O
Shibata, T
Yokoyama, S
机构
[1] RIKEN Genom Sci Ctr, Yokohama, Kanagawa 2300045, Japan
[2] Univ Tokyo, Grad Sch Sci, Dept Biophys & Biochem, Bunkyo Ku, Tokyo 1130033, Japan
[3] SPring 8, RIKEN Harima Inst, Cellular Signaling Lab, Sayo, Hyogo 6795148, Japan
[4] RIKEN, Cellular & Mol Biol Lab, Wako, Saitama 3510198, Japan
基金
日本科学技术振兴机构;
关键词
D O I
10.1016/S1097-2765(02)00587-7
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The human Rad52 protein forms a heptameric ring that catalyzes homologous pairing. The N-terminal half of Rad52 is the catalytic domain for homologous pairing and the ring formed by the domain fragment was reported to be approximately decameric. Splicing variants of Rad52 and a yeast homolog (Rad59) are composed mostly of this domain. In this study, we determined the crystal structure of the homologous-pairing domain of human Rad52 and revealed that the domain forms an undecameric ring. Each monomer has a beta-beta-beta-alpha fold, which consists of highly conserved amino acid residues among Rad52 homologs. A mutational analysis revealed that the amino acid residues located between the beta-beta-beta-alpha fold and the characteristic hairpin loop are essential for ssDNA and dsDNA binding.
引用
收藏
页码:359 / 371
页数:13
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