Authors: | Liu, J.; Marians, K. J. |
Article Title: | PriA-directed assembly of a primosome on D loop DNA |
Abstract: | Escherichia coli strains carrying null mutations in priA are chronically induced for the SOS response and are defective in homologous recombination, repair of UV damaged DNA, double-strand break repair, and both induced and constitutive stable DNA replication. This led to the proposal that PriA directed replication fork assembly at D loops formed by the homologous recombination machinery. The demonstration that PriA specifically recognized and bound D loop DNA supported this hypothesis. Using DNA footprinting as an assay, we show here that PriA also directs the assembly of a φX174-type primosome on D loop DNA. The ability to load a complete primosome on D loop DNA is a step necessary for replication fork assembly. |
Keywords: | controlled study; unclassified drug; dna-binding proteins; nonhuman; dna replication; dna recombination; complex formation; protein dna binding; molecular dynamics; dna; double stranded dna; molecular sequence data; recombination, genetic; molecular recognition; escherichia coli; base sequence; excision repair; helicase; dna, single-stranded; nucleic acid conformation; enzyme specificity; bacterial dna; adenosine triphosphatases; reaction analysis; dna helicases; concentration response; dna cleavage; escherichia coli proteins; electrophoresis, polyacrylamide gel; dna conformation; dna strand; dna footprinting; deoxyribonuclease i; priority journal; article; enzyme pria; aspergillus nuclease s1 |
Journal Title: | Journal of Biological Chemistry |
Volume: | 274 |
Issue: | 35 |
ISSN: | 0021-9258 |
Publisher: | American Society for Biochemistry and Molecular Biology |
Date Published: | 1999-08-27 |
Start Page: | 25033 |
End Page: | 25041 |
Language: | English |
DOI: | 10.1074/jbc.274.35.25033 |
PUBMED: | 10455182 |
PROVIDER: | scopus |
DOI/URL: | |
Notes: | Article -- Export Date: 16 August 2016 -- Source: Scopus |