The cohesin-like RecN protein stimulates RecA-mediated recombinational repair of DNA double-strand breaks.
| Autor: | Uranga LA; Department of Chemistry and Biochemistry, New Mexico State University, P.O. Box 30001, MSC 3C, Las Cruces, New Mexico 88003, USA., Reyes ED; Department of Chemistry and Biochemistry, New Mexico State University, P.O. Box 30001, MSC 3C, Las Cruces, New Mexico 88003, USA., Patidar PL; Department of Chemistry and Biochemistry, New Mexico State University, P.O. Box 30001, MSC 3C, Las Cruces, New Mexico 88003, USA., Redman LN; Department of Chemistry and Biochemistry, New Mexico State University, P.O. Box 30001, MSC 3C, Las Cruces, New Mexico 88003, USA., Lusetti SL; Department of Chemistry and Biochemistry, New Mexico State University, P.O. Box 30001, MSC 3C, Las Cruces, New Mexico 88003, USA. |
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| Jazyk: | angličtina |
| Zdroj: | Nature communications [Nat Commun] 2017 May 17; Vol. 8, pp. 15282. Date of Electronic Publication: 2017 May 17. |
| DOI: | 10.1038/ncomms15282 |
| Abstrakt: | 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. |
| Databáze: | MEDLINE |
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