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J. Biol. Chem., Vol. 276, Issue 37, 35201-35208, September 14, 2001
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§,
¶,
,
§¶**, and

From the 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.
RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan, the ¶ Cellular
Signaling Laboratory, RIKEN Harima Institute at Spring-8, 1-1-1 Kohto,
Mikazuki-cho, Sayo, Hyogo 679-5143, Japan, the
Cellular and
Molecular Biology Laboratory, RIKEN, 2-1 Hirosawa, Wako, Saitama
351-0198, Japan, and the § Department of Biophysics and
Biochemistry, Graduate School of Science, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.

To whom correspondence may be addressed.
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