Homologous Pairing Promoted by the Human, Rad52 Protein

Wataru Kagawa, Hitoshi Kurumizaka, Shukuko Ikawa, Shigeyuki Yokoyama*, Takehiko Shibata

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

127 Citations (Scopus)


The Rad52 protein, which is unique to eukaryotes, plays important roles in the Rad51-dependent and the Rad51-independent pathways of DNA recombination. In the present study, we have biochemically characterized the homologous pairing activity of the HsRad52 protein (Homo sapiens Rad52) and found that the presynaptic complex formation with ssDNA is essential in its catalysis of homologous pairing. We have identified an N-terminal fragment (amino acid residues 1-237, HsRad521-237) that is defective in binding to the human Rad51 protein, which catalyzed homologous pairing as efficiently as the wild type HsRad52. Electron microscopic visualization revealed that HsRad52 and HsRad521-237 both formed nucleoprotein filaments with single-stranded DNA. These lines of evidence suggest the role of HsRad52 in the homologous pairing step of the Rad51-independent recombination pathway. Our results reveal the striking similarity between HsRad52 and the Escherichia coli RecT protein, which functions in a RecA-independent recombination pathway.

Original languageEnglish
Pages (from-to)35201-35208
Number of pages8
JournalJournal of Biological Chemistry
Issue number37
Publication statusPublished - 2001 Sept 14
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry


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