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

Wataru Kagawa, Hitoshi Kurumizaka, Ryuichiro Ishitani, Shuya Fukai, Osamu Nureki, Takehiko Shibata, Shigeyuki Yokoyama

研究成果: Article査読

156 被引用数 (Scopus)

抄録

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 β-β-β-α fold, which consists of highly conserved amino acid residues among Rad52 homologs. A mutational analysis revealed that the amino acid residues located between the β-β-β-α fold and the characteristic hairpin loop are essential for ssDNA and dsDNA binding.

本文言語English
ページ(範囲)359-371
ページ数13
ジャーナルMolecular Cell
10
2
DOI
出版ステータスPublished - 2002 8
外部発表はい

ASJC Scopus subject areas

  • 分子生物学

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