PMID:15576682
| Citation |
Cadman, CJ and McGlynn, P (2004) PriA helicase and SSB interact physically and functionally. Nucleic Acids Res. 32:6378-87 |
|---|---|
| Abstract |
PriA helicase is the major DNA replication restart initiator in Escherichia coli and acts to reload the replicative helicase DnaB back onto the chromosome at repaired replication forks and D-loops formed by recombination. We have discovered that PriA-catalysed unwinding of branched DNA substrates is stimulated specifically by contact with the single-strand DNA binding protein of E.coli, SSB. This stimulation requires binding of SSB to the initial DNA substrate and is effected via a physical interaction between PriA and the C-terminus of SSB. Stimulation of PriA by the SSB C-terminus may act to ensure that efficient PriA-catalysed reloading of DnaB occurs only onto the lagging strand template of repaired forks and D-loops. Correlation between the DNA repair and recombination defects of strains harbouring an SSB C-terminal mutation with inhibition of this SSB-PriA interaction in vitro suggests that SSB plays a critical role in facilitating PriA-directed replication restart. Taken together with previous data, these findings indicate that protein-protein interactions involving SSB may coordinate replication fork reloading from start to finish. |
| Links |
PubMed PMC535688 Online version:10.1093/nar/gkh980 |
| Keywords |
Adenosine Triphosphatases/metabolism; Binding Sites; DNA/chemistry; DNA/metabolism; DNA Helicases/metabolism; DNA, Single-Stranded/metabolism; DNA-Binding Proteins/chemistry; DNA-Binding Proteins/metabolism; DnaB Helicases; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism |
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