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Nucleic Acids Research, Vol 25, Issue 14 2766-2772, Copyright © 1997 by Oxford University Press

ARTICLES

Purification and characterization of the RecF protein from Bacillus subtilis 168

S Ayora and JC Alonso
Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autonoma de Madrid, Cantoblanco, 28049 Madrid, Spain.

Genetic evidence suggests that the Bacillus subtilis recF gene product is involved in DNA repair and recombination. The RecF protein was overproduced and purified. NH2-terminal protein sequence analysis of RecF was consistent with the deduced amino acid sequence of the recF gene. The RecF protein (predicted molecular mass 42.3 kDa) bound single- and double-stranded DNA in a filter binding and in a gel retarding assay. The RecF-ssDNA or -dsDNA complex formation proceeds in the absence of nucleotide cofactors. RecF-ssDNA interaction is markedly stimulated by divalent cations. The apparent equilibrium constants of the RecF-DNA complexes are approximately 110-130 nM for both ssDNA and dsDNA. The binding reaction shows no cooperativity. The RecF protein does not physically interact with the RecR protein. Under our experimental conditions an ATPase activity was not associated with the purified RecF protein or with the RecF and RecR proteins.
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