Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Inactivation of the Escherichia coli priA DNA replication protein induces the SOS response.

Journal of bacteriology - 1 Nov 1991

Nurse P, Zavitz K H, Marians K J

Abstract excerpt

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 phi X174 complementary-strand...

Topics

Bacterial Proteins
Blotting, Southern
DNA Replication
DNA, Bacterial
Escherichia coli
Genes, Bacterial
Mutagenesis, Insertional
Phenotype
SOS Response, Genetics

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Open in PubMed Open full text

Identifiers

PMID: 1938875
DOI: 10.1128/jb.173.21.6686-6693.1991
PMCID: PMC209016

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1938875-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Inactivation of the Escherichia coli priA DNA replication protein induces the SOS response.PMID 1938875Read ↗

ATPase-deficient mutants of the Escherichia coli DNA replication protein PriA are capable of catalyzing the assembly of active primosomes.Semantic proximity Read ↗

dnaC mutations suppress defects in DNA replication- and recombination-associated functions in priB and priC double mutants in Escherichia coli K-12.Semantic proximity Read ↗

Differential suppression of priA2::kan phenotypes in Escherichia coli K-12 by mutations in priA, lexA, and dnaC.Semantic proximity Read ↗

The DNA replication priming protein, PriA, is required for homologous recombination and double-strand break repair.Semantic proximity Read ↗

Mutational Analysis of Residues in PriA and PriC Affecting Their Ability To Interact with SSB in Escherichia coli K-12.Semantic proximity Read ↗

Escherichia coli K-12 has two distinguishable PriA-PriB replication restart pathways.Semantic proximity Read ↗

PriA mutations that affect PriA-PriC function during replication restart.Semantic proximity Read ↗

Escherichia coli PriA protein is essential for inducible and constitutive stable DNA replication.Semantic proximity Read ↗

Restart of DNA replication in Gram-positive bacteria: functional characterisation of the Bacillus subtilis PriA initiator.Semantic proximity Read ↗

ATPase/helicase motif mutants of Escherichia coli PriA protein essential for recombination-dependent DNA replication.Semantic proximity Read ↗

DnaB, DnaD and DnaI proteins are components of the Bacillus subtilis replication restart primosome.Semantic proximity Read ↗

Replication restart in gyrB Escherichia coli mutants.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.