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

The RdgC protein employs a novel mechanism involving a finger domain to bind to circular DNA.

Nucleic acids research - 1 Oct 2010

Briggs Geoffrey S, Yu Jing, Mahdi Akeel A, Lloyd Robert G

Abstract excerpt

The DNA-binding protein RdgC has been identified as an inhibitor of RecA-mediated homologous recombination in Escherichia coli. In Neisseria species, RdgC also has a role in virulence-associated antigenic variation. We have previously solved the crystal structure of the E. coli RdgC protein and shown it to form a toroidal dimer. In this study, we have conducted a mutational analysis of residues proposed to...

Read the complete abstract on PubMed

Topics

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

Share to Dimerization
Share to DNA, Circular
Share to DNA Helicases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Escherichia coli

Share to Escherichia coli Proteins

Share to Gene Deletion

Share to Plasmids

Share to Protein Structure, Tertiary

Source

Open in PubMed Open full text

Identifiers

PMID: 20525790
DOI: 10.1093/nar/gkq509
PMCID: PMC2965237

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

The RdgC protein employs a novel mechanism involving a finger domain to bind to circular DNA.PMID 20525790Read ↗

Characterization of the Neisseria meningitidis Helicase RecG.Semantic proximity Read ↗

The crystal structure of bacteriophage λ RexA provides novel insights into the DNA binding properties of Rex-like phage exclusion proteins.Semantic proximity Read ↗

The RdgC protein of Escherichia coli binds DNA and counters a toxic effect of RecFOR in strains lacking the replication restart protein PriA.Semantic proximity Read ↗

Conferring substrate specificity to DNA helicases: role of the RecQ HRDC domain.Semantic proximity Read ↗

Biochemical characterization of RecBCD enzyme from an Antarctic Pseudomonas species and identification of its cognate Chi (χ) sequence.Semantic proximity Read ↗

Structural insights into the unique single-stranded DNA-binding mode of Helicobacter pylori DprASemantic proximity Read ↗

RdgB acts to avoid chromosome fragmentation in Escherichia coli.Semantic proximity Read ↗

Construction of recB-recD genetic fusion and functional analysis of RecBDC fusion enzyme in Escherichia coli.Semantic proximity Read ↗

Altering the Neisseria gonorrhoeae pilE Guanine Quadruplex Loop Bases Affects Pilin Antigenic Variation.Semantic proximity Read ↗

A homologue of the recombination-dependent growth gene, rdgC, is involved in gonococcal pilin antigenic variation.Semantic proximity Read ↗

RecR forms a ring-like tetramer that encircles dsDNA by forming a complex with RecF.Semantic proximity Read ↗

Both OB folds of single-stranded DNA-binding protein are essential for its ssDNA binding activity in Deinococcus radiodurans.Semantic proximity Read ↗

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