Inactivation of the Escherichia coli PriA DNA replication protein induces the SOS response Journal Article
| Authors: | Nurse, P.; Zavitz, K. H.; Marians, K. J. |
| Article Title: | Inactivation of the Escherichia coli PriA DNA replication protein induces the SOS response |
| Abstract: | Many of the proteins that operate at the replication fork in Escherichia coli have been defined genetically. These include some of the subunits of the DNA polymerase III holoenzyme, the DnaB replication fork helicase, and the DnaG primase. The multiprotein primosome (which includes the DnaB and DnaG proteins), defined biochemically on the basis of its requirement during bacteriophage φX174 complementary-strand synthesis, could serve as the helicase-primase replication machine on the lagging-strand template. In order to determine if this is the case, we have gebun an investigation of the phenotypes of mutants with mutations priA, priB, and priC, which encode the primosomal proteins factor Y (protein n'), n, and n'', respectively. Inactivation of priA by insertional mutagenesis resulted in the induction of the SOS response, as evinced by induction of a resident λ prophage, extreme filamentation, and derepression of an indicator operon in which β-galactosidase production was controlled by the dinD1 promoter. In addition, the copy numbers of resident pBR322 plasmids were reduced four- to fivefold in these strains, and production of φX174 phage was delayed considerably. These results are discussed in the context of existing models for SOS induction and possible roles for the PriA protein at the replication fork in vivo. |
| Keywords: | signal transduction; mutation; nonhuman; dna polymerase; dna replication; escherichia coli; plasmid; beta galactosidase; southern blotting; bacteriophage; priority journal; article |
| Journal Title: | Journal of Bacteriology |
| Volume: | 173 |
| Issue: | 21 |
| ISSN: | 0021-9193 |
| Publisher: | American Society for Microbiology |
| Date Published: | 1991-11-01 |
| Start Page: | 6686 |
| End Page: | 6693 |
| Language: | English |
| DOI: | 10.1128/jb.173.21.6686-6693.1991 |
| PUBMED: | 1938875 |
| PROVIDER: | scopus |
| PMCID: | PMC209016 |
| DOI/URL: | |
| Notes: | Article -- Export Date: 27 September 2019 -- Source: Scopus |
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