Discover Community Create You

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

A structural model of the PriB-DnaT complex in Escherichia coli replication restart.

FEBS letters - 1 Feb 2021

Abe Yoshito, Ikeda Yohei, Fujiyama Saki, Kini R Manjunatha, Ueda Tadashi

Abstract excerpt

In Escherichia coli, DNA replication is restarted following DNA repair by the PriA-dependent pathway, in which the binding and dissociation of proteins such as PriA, PriB, and DnaT on ssDNA lead to the formation of a protein-DNA complex for recruiting the DnaB-DnaC replication protein complex. However, the structure of the PriB-DnaT complex, which is an essential step in the PriA-dependent pathway, remains...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to DNA Replication
Share to DNA, Single-Stranded
Share to Molecular Dynamics Simulation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Peptides

Share to Protein Conformation, alpha-Helical

Share to Protein Conformation, beta-Strand

Share to Protein Interaction Domains and Motifs

Share to Thermodynamics

Source

Identifiers

PMID: 33275781
DOI: 10.1002/1873-3468.14020

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

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A structural model of the PriB-DnaT complex in Escherichia coli replication restart.PMID 33275781Read ↗

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

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

Replication Restart in Bacteria.Semantic proximity Read ↗

Crystal structure and DNA-binding mode of Klebsiella pneumoniae primosomal PriB protein.Semantic proximity Read ↗

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

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

Purification and characterization of DnaC810, a primosomal protein capable of bypassing PriA function.Semantic proximity Read ↗

Functional interplay between the Bacillus subtilis DnaD and DnaB proteins essential for initiation and re-initiation of DNA replication.Semantic proximity Read ↗

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

Replication Protein A, the Main Eukaryotic Single-Stranded DNA Binding Protein, a Focal Point in Cellular DNA MetabolismSemantic proximity Read ↗

A novel dnaC mutation that suppresses priB rep mutant phenotypes in Escherichia coli K-12.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 ↗

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