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Nucleic Acids Research, 1994, Vol. 22, No. 16 3387-3391
© 1994

MOLECULAR BIOLOGY

A chimeric Rec-A protein that implicates non-Watson-Crick interactions in homologous pairing

Hitoshi Kurumizaka1,2, B.J. Rao3, Tomoko Ogawa4, Charles M. Radding3 and Takehiko Shibata1,2,*

1laboratory of Cellular and Molecular Biology, The Institute of Physical and Chemical Research(RIKEN) Wako-shi, Saitama 351-01, 2The Graduate School of Science and Engineering, Saitama University Urawa-shi, Saitama 338, Japan 3Department of Genetics and Molecular Biophysics and Biochemistry, Yale University School of Medicine New Haven, CT 06510, USA 4Department of Biology, Faculty of Science, Osaka University Toyonaka, Osaka 560, Japan

*To whom correspondence should be addressed at: Laboratory of Cellular and Molecular Biology, The Institute of Physical and Chemical Research (RIKEN), Wako-shi, Saitama 351-01, Japan

Received May 6, 1994. Revised July 14, 1994. Accepted July 14, 1994.

The helical filament formed by RecA protein on singlestranded DNA plays an important role in homologous recombination and pairs with a complementary single strand or homologous duplex DNA. The RecA nucleoprotein filament also recognizes an identical single strand. The chimeric protein, RecAc38, forms a nucleoprotein filament that recognizes a complementary strand but is defective in recognition of duplex DNA, and is associated with phenotypic defects in repair and recombination. As described here, RecAc38 nucleoprotein filament is also defective in recognition of an identical strand, either when the filament has within it a single strand or duplex DNA. A model that postulates three DNA binding sites rationalizes these observations and suggests that the third binding site mediates non- Watson-Crick interactions that are instrumental in recognition of homology in duplex DNA.


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