The cohesin-like RecN protein stimulates RecA-mediated recombinational repair of DNA double-strand breaks

Lee A. Uranga, Emigdio D. Reyes, Praveen L. Patidar, Lindsay N. Redman and Shelley L. Lusetti ()
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Lee A. Uranga: New Mexico State University
Emigdio D. Reyes: New Mexico State University
Praveen L. Patidar: New Mexico State University
Lindsay N. Redman: New Mexico State University
Shelley L. Lusetti: New Mexico State University

Nature Communications, 2017, vol. 8, issue 1, 1-11

Abstract: Abstract RecN is a cohesin-like protein involved in DNA double-strand break repair in bacteria. The RecA recombinase functions to mediate repair via homologous DNA strand invasion to form D-loops. Here we provide evidence that the RecN protein stimulates the DNA strand invasion step of RecA-mediated recombinational DNA repair. The intermolecular DNA tethering activity of RecN protein described previously cannot fully explain this novel activity since stimulation of RecA function is species-specific and requires RecN ATP hydrolysis. Further, DNA-bound RecA protein increases the rate of ATP hydrolysis catalysed by RecN during the DNA pairing reaction. DNA-dependent RecN ATPase kinetics are affected by RecA protein in a manner suggesting a specific order of protein–DNA assembly, with RecN acting after RecA binds DNA. We present a model for RecN function that includes presynaptic stimulation of the bacterial repair pathway perhaps by contributing to the RecA homology search before ternary complex formation.

Date: 2017
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DOI: 10.1038/ncomms15282

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