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Nucleic Acids Research, 1992, Vol. 20, No. 16 4339-4346
© 1992

MOLECULAR BIOLOGY

RNA-DNA hybridization promoted by E.coli RecA portein

Dwight P. Kirkpatirck, B. Jagdeeshwar Rao and Charles M. Radding*

Department of Molecular Biophysics and Biochemistry and Department of Genetics, Yale University School of Medicine New Haven, CT 06510, USA

*To whom correspondence should be addressed

Received March 11, 1992. Revised July 15, 1992. RecA protein of E.coli plays a central regulatory role that is induced by damage to DNA and results in the inactivation of LexA repressor. In vitro, RecA protein binds preferentially to single-stranded DNA to form a nucleoprotein filament that can recognize homology in naked duplex DNA and promote extensive strand exchange. Although RecA protein shows little tendency at neutral pH to bind to RNA, we found that It nonetheless catalyzed at 37°C the hybridization of complementary RNA and single-stranded DNA sequences. Hybrids made by RecA protein at 37°C appeared indistinguishable from ones prepared by thermal annealing. RNA-DNA hybridization by RecA protein at neutral pH required, as does RecA-promoted homologous pairing, optimal conditions for the formation of RecA nucleoprotein filaments. The cosedimentation of RNA with those filaments further paralleled observations made on the formation of networks of nucleoprotein filaments with doublestranded DNA, an Instrumental intermediate in homologous pairing In vitro. These similarities with the pairing reaction support the view that RecA protein acts specifically in the hybridization reaction.


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