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Article

Basic and aromatic residues in the C-terminal domain of PriC are involved in ssDNA and SSB binding.

Journal of biochemistry - 1 Jun 2015

Aramaki Takahiko, Abe Yoshito, Furutani Kaori, Katayama Tsutomu, Ueda Tadashi

Abstract excerpt

In bacterial organisms, the oriC-independent primosome plays an essential role in replication restart after dissociation of the replication DNA-protein complex following DNA damage. PriC is a key protein component in the oriC-independent replication restart primosome. Our previous study suggested that PriC was divided into an N-terminal domain and a C-terminal domain, with the latter domain being the major...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 25701026
DOI: 10.1093/jb/mvv014

Genes

SSB

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Basic and aromatic residues in the C-terminal domain of PriC are involved in ssDNA and SSB binding.PMID 25701026Read ↗

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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 ↗

Complexed crystal structure of replication restart primosome protein PriB reveals a novel single-stranded DNA-binding mode.Semantic proximity Read ↗

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

A critical role of the 3' terminus of nascent DNA chains in recognition of stalled replication forks.Semantic proximity Read ↗

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

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

Essential role of the iron-sulfur cluster binding domain of the primase regulatory subunit Pri2 in DNA replication initiation.Semantic proximity Read ↗

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