PMID:10713144: Difference between revisions
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!align=left |Citation | |||
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'''Xu, L and Marians, KJ''' (2000) Purification and characterization of DnaC810, a primosomal protein capable of bypassing PriA function. ''J. Biol. Chem.'' '''275''':8196-205 | |||
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!align=left |Abstract | |||
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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. | |||
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=10713144 PubMed] | |||
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| | !align=left |Keywords | ||
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|- | 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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==Significance {{HelpIcon|Help:Literature}} == | ==Significance {{HelpIcon|Help:Literature}} == | ||
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==Annotations {{HelpIcon|Help:Literature}}== | ==Annotations {{HelpIcon|Help:Literature}}== | ||
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==EcoliWiki Links {{HelpIcon|Help:Literature}} == | ==EcoliWiki Links {{HelpIcon|Help:Literature}} == | ||
Latest revision as of 04:11, 15 September 2013
| Citation |
Xu, L and Marians, KJ (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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