Inhibition of RecA protein function by the RdgC protein from Eschericia coli

doi:10.1074/jbc.M513592200

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Papers In Press, published online ahead of print December 22, 2005
J. Biol. Chem, 10.1074/jbc.M513592200
Submitted on December 21, 2005
Accepted on December 22, 2005

Inhibition of RecA protein function by the RdgC protein from Eschericia coli

Julia C. Drees, Sindhu Chitteni-Pattu, Darrell R. McCaslin, Ross B. Inman, and Michael M. Cox

Department of Biochemistry, University of Wisconsin - Madison, Madison, WI 53706-1544

Corresponding Author: COX{at}BIOCHEM.WISC.EDU

The Escherichia coli RdgC protein is a potential negative regulator of RecA function. RdgC inhibits RecA protein-promoted DNA strand exchange, ATPase activity, and RecA-dependent LexA cleavage. The primary mechanism of RdgC inhibition appears to involve a simple competition for DNA binding sites, especially on duplex DNA. The capacity of RecA to compete with RdgC is improved by the DinI protein. RdgC protein can inhibit DNA strand exchange catalyzed by RecA nucleoprotein filaments formed on single stranded DNA by binding to the homologous duplex DNA and thereby blocking access to that DNA by the RecA nucleoprotein filaments. RdgC protein binds to single stranded and double stranded DNA and the protein can be visualized on DNA using electron microscopy. RdgC protein exists in solution as a mixture of oligomeric states in equilibrium, most likely monomers, dimers and tetramers. This concentration-dependent change of state appears to affect its mode of binding to DNA and its capacity to inhibit RecA. The various species differ in their capacity to inhibit RecA function.

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