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- W2127979283 abstract "RecG and RuvAB are proposed to act at stalled DNA replication forks to facilitate replication restart. To define the roles of these proteins in fork regression, we used a combination of assays to determine whether RecG, RuvAB or both are capable of acting at a stalled fork. The results show that RecG binds to the C-terminus of single-stranded DNA binding protein (SSB) forming a stoichiometric complex of 2 RecG monomers per SSB tetramer. This binding occurs in solution and to SSB protein bound to single stranded DNA (ssDNA). The result of this binding is stabilization of the interaction of RecG with ssDNA. In contrast, RuvAB does not bind to SSB. Side-by-side analysis of the catalytic efficiency of the ATPase activity of each enzyme revealed that (-)scDNA and ssDNA are potent stimulators of the ATPase activity of RecG but not for RuvAB, whereas relaxed circular DNA is a poor cofactor for RecG but an excellent one for RuvAB. Collectively, these data suggest that the timing of repair protein access to the DNA at stalled forks is determined by the nature of the DNA available at the fork. We propose that RecG acts first, with RuvAB acting either after RecG or in a separate pathway following protein-independent fork regression." @default.
- W2127979283 created "2016-06-24" @default.
- W2127979283 creator A5036019614 @default.
- W2127979283 creator A5060644426 @default.
- W2127979283 creator A5060925000 @default.
- W2127979283 date "2008-11-05" @default.
- W2127979283 modified "2023-09-25" @default.
- W2127979283 title "RecG interacts directly with SSB: implications for stalled replication fork regression" @default.
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- W2127979283 doi "https://doi.org/10.1093/nar/gkn795" @default.
- W2127979283 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2602778" @default.
- W2127979283 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/18986999" @default.
- W2127979283 hasPublicationYear "2008" @default.
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