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The Bacterial RecA Protein: Structure, Function, and Regulation

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Molecular Genetics of Recombination

Part of the book series: Topics in Current Genetics ((TCG,volume 17))

Abstract

The bacterial RecA protein is the prototypical recombinase, promoting the central steps of DNA pairing and strand exchange in genetic recombination and recombinational DNA repair. RecA homologs are present in virtually all organisms from bacteria to humans. RecA is a multifunctional protein. As a recombinase, the protein binds to DNA in the form of a helical filament, and exhibits a DNA-dependent ATPase activity. As a nucleoprotein filament, RecA promotes a series of easily monitored DNA strand exchange reactions in vitro. In addition to its role as a recombinase, the E. coliRecA protein is also a key component of the regulatory system that controls the induction of the SOS response, and it plays a direct role in the UV mutagenesis promoted by DNA polymerase V. RecA protein is subject to multiple layers of regulation. RecA is autoregulated by its own C-terminus. Many other proteins, including the RecF, RecO, RecR, DinI, RecX, RdgC, PsiB, and SSB proteins, have either a demonstrated or probable role in modulating where and when RecA-mediated recombination events occur.

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  1. Department of Biochemistry, University of Wisconsin-Madison, 433 Babcock Drive, Madison, Wisconsin, USA

    Michael M. Cox

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Cox, M.M. (2006). The Bacterial RecA Protein: Structure, Function, and Regulation. In: Aguilera, A., Rothstein, R. (eds) Molecular Genetics of Recombination. Topics in Current Genetics, vol 17. Springer, Berlin, Heidelberg. https://doi.org/10.1007/4735_2006_0205

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