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Nucleic Acids Research, 1990, Vol. 18, No. 9 2707-2714
© 1990

CHEMISTRY

Interaction of RecA protein with pBR322 DNA modified by N-hydroxy-2-acetylaminofluorene and 4-hydroxyaminoquinoline 1-oxide

Misaki Kojima, Makoto Suzuki1, Toshiteru Morita2, Tomoko Ogawa3, Hideyuki Ogawa3 and Mariko Tada*

Laboratory of Biochemistry, Aichi Cancer Center Research Institute Kanokoden Chikusa-ku, Nagoya 464, Japan 1Faculty of Pharmaceutical Science, Nagoya City University Tanabedori Mizuho-ku, Nagoya 467, Japan 2Department of Biology, College of General Education Toyonaka, Osaka 560, Japan 3Department of Biology, Faculty of Science, Osaka University Tanabedori Mizuho-ku, Nagoya 467, Japan

*To whom correspondence should be addressed

Received January 4, 1990. Accepted April 10, 1990.

Interaction of RecA protein of Eschehchia coli with pBR322 DNA modified by N-hydroxy-2-acetylaminofluorene (N-OH-AAF) and 4-hydroxyamlnoqulnollne 1-oxide (4HAQO) was investigated. RecA protein bound more efficiently to modified DNA than to unmodified DNA as judged by filter-binding and gel electrophoresis assay. The binding of RecA protein with modified DNA resulted in the stimulation of ATPase activity and the activation for RecA protein to stimulate the repressor cleavage. These abilities of RecA protein were increased proportionally to the number of adducts In the plasmid DNA ( 0–5 adducts). Apurinic and alkyiated DNA did not activate RecA protein. We suggest that modification of DNA by N-OH-AAF and 4HAQO provides binding sites for RecA protein and may act as an activation signal for SOS response.


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