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

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Abstract

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.

Original languageEnglish
Pages (from-to)359-371
Number of pages13
JournalMolecular Cell
Volume10
Issue number2
DOIs
Publication statusPublished - 2002 Aug
Externally publishedYes

ASJC Scopus subject areas

  • Molecular Biology

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    Kagawa, W., Kurumizaka, H., Ishitani, R., Fukai, S., Nureki, O., Shibata, T., & Yokoyama, S. (2002). Crystal structure of the homologous-pairing domain from the human Rad52 recombinase in the undecameric form. Molecular Cell, 10(2), 359-371. https://doi.org/10.1016/S1097-2765(02)00587-7