PMID:10713144
| Citation |
No author listed (2000) Purification and characterization of DnaC810, a primosomal protein capable of bypassing PriA function. J. Biol. Chem. 275:8196-205 |
|---|---|
| Abstract |
Escherichia coli strains lacking PriA are severely compromised in their ability to repair UV-damaged DNA and to perform homologous recombination. These phenotypes arise because of a lack of PriA-directed replication fork assembly at recombination intermediates such as D-loops. Naturally arising suppressor mutations in dnaC restore strains carrying the priA2::kan null allele to wild-type function. We have cloned one such gene, dnaC810, and overexpressed, purified, and characterized the DnaC810 protein. DnaC810 can support a PriA-independent synthesis of phiX174 complementary strand DNA. This can be attributed to its ability, unlike wild-type DnaC, to catalyze a SSB-insensitive general priming reaction with DnaB and DnaG on any SSB-coated single-stranded DNA. Gel mobility shift analysis revealed that DnaC810 could load DnaB directly to SSB-coated single-stranded DNA as well as to D loop DNA. This explains the ability of DnaC810 to bypass the requirement for PriA, PriB, PriC, and DnaT during replication fork assembly at recombination intermediates. |
| Links | |
| Keywords |
Bacterial Proteins/genetics; Bacterial Proteins/isolation & purification; Bacterial Proteins/metabolism; Bacteriophage phi X 174/genetics; DNA Helicases/metabolism; DNA Replication; DNA, Single-Stranded/metabolism; DNA-Binding Proteins/metabolism; DnaB Helicases; Escherichia coli/virology; Escherichia coli Proteins; Mutation; Protein Binding; Recombinant Proteins/isolation & purification; Recombinant Proteins/metabolism; Replication Protein A; Suppression, Genetic |
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