Replication fork assembly at recombination intermediates is required for bacterial growth Journal Article
| Authors: | Liu, J.; Xu, L.; Sandler, S. J.; Marians, K. J. |
| Article Title: | Replication fork assembly at recombination intermediates is required for bacterial growth |
| Abstract: | PriA, a 3' → 5' DNA helicase, directs assembly of a primosome on some bacteriophage and plasmid DNAs. Primosomes are multienzyme replication machines that contribute both the DNA-unwinding and Okazaki fragment-priming functions at the replication fork. The role of PriA in chromosomal replication is unclear. The phenotypes of priA null mutations suggest that the protein participates in replication restart at recombination intermediates. We show here that PriA promotes replication fork assembly at a D loop, an intermediate formed during initiation of homologous recombination. We also show that DnaC810, encoded by a naturally arising intergenic suppressor allele of the prid2::kan mutation, bypasses the need for PriA during replication fork assembly at D loops in vitro. These findings underscore the essentiality of replication fork restart at recombination intermediates under normal growth conditions in bacteria. |
| Keywords: | unclassified drug; gene mutation; dna-binding proteins; nonhuman; dna replication; dna synthesis; enzyme activity; bacteria (microorganisms); genetic recombination; molecular sequence data; recombination, genetic; escherichia coli; base sequence; helicase; dna replication origin; replication protein a; chromosome replication; enzyme; bacterial growth; oligodeoxyribonucleotides; bacteria; primosome; open reading frames; templates, genetic; negibacteria; dna polymerase iii; bacteriophage phi x 174; priority journal; article; unidentified bacteriophage |
| Journal Title: | Proceedings of the National Academy of Sciences of the United States of America |
| Volume: | 96 |
| Issue: | 7 |
| ISSN: | 0027-8424 |
| Publisher: | National Academy of Sciences |
| Date Published: | 1999-03-01 |
| Start Page: | 3552 |
| End Page: | 3555 |
| Language: | English |
| DOI: | 10.1073/pnas.96.7.3552 |
| PUBMED: | 10097074 |
| PROVIDER: | scopus |
| PMCID: | PMC22331 |
| DOI/URL: | |
| Notes: | Article -- Export Date: 16 August 2016 -- Source: Scopus |
