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© 1993 Oxford University Press

other

Enhancement of binding rate of RecA protein to DNA by carcinogenic benzo[a]pyrene derivatives and selective change of adduct conformation

Seog K. Kim, Masayuki Takahashi 1, Bengt Jernström 2 and Bengt Nordén 2

Department of Physical Chemistry, Chalmers University of Technology S 412-96 Gothenburg, Sweden
1Groupe de Carcérogenèse et de Mutagenèse Moléculaire et Structurale, Institut de Biologie Moléculaire et Celluaire du CNRS F-67084 Strasbourg, France
2Department of Toxicology Karolinska Institute Box 60400, S-104 01 Stockholm, Sweden

The association kinetics of RecA protein from Escherichia coli to DNA is strongly enhanced if even a minor fraction of DNA bases has been modified by a carcinogenic (+)-anti metabolite of benzo[a]pyrene (BPDE). The enhancement is much smaller with the less carcinogenic (–)-anti enantiomer of BPDE suggesting the possibility that the RecA protein binds selectively to the proto-oncogenic target. Most importantly, the binding of RecA to DNA modified with the latter enantiomer is found to give rise to a reorganization of this BPDE adduct from an intercalation site into a minor groove site. This indicates that the binding mechanism of RecA is via intercalation of some amino acid moiety, a discovery that could explain the ~50% contour length increase of the DNA within its fibrous complex with RecA.


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