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 acidic C-terminal tail of the GyrA subunit moderates the DNA supercoiling activity of Bacillus subtilis gyrase.

The Journal of biological chemistry - 2 May 2014

Lanz Martin A, Farhat Mohamad, Klostermeier Dagmar

Abstract excerpt

Gyrase is a type II DNA topoisomerase that introduces negative supercoils into DNA in an ATP-dependent reaction. It consists of a topoisomerase core, formed by the N-terminal domains of the two GyrA subunits and by the two GyrB subunits, that catalyzes double-stranded DNA cleavage and passage of a second double-stranded DNA through the gap in the first. The C-terminal domains (CTDs) of the GyrA subunits form a...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphate
Share to Bacillus subtilis

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to DNA Gyrase

Share to DNA, Superhelical

Share to Fluorescence Polarization

Share to Fluorescence Resonance Energy Transfer

Share to Hydrolysis

Share to Protein Subunits

Source

Open in PubMed Open full text

Identifiers

PMID: 24563461
DOI: 10.1074/jbc.M114.547745
PMCID: PMC4007426

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The acidic C-terminal tail of the GyrA subunit moderates the DNA supercoiling activity of Bacillus subtilis gyrase.PMID 24563461Read ↗

The GyrA-box determines the geometry of DNA bound to gyrase and couples DNA binding to the nucleotide cycle.Semantic proximity Read ↗

The "GyrA-box" is required for the ability of DNA gyrase to wrap DNA and catalyze the supercoiling reaction.Semantic proximity Read ↗

Modulated control of DNA supercoiling balance by the DNA-wrapping domain of bacterial gyrase.Semantic proximity Read ↗

The pivot point arginines identified in the β-pinwheel structure of C-terminal domain from Salmonella Typhi DNA Gyrase A subunit.Semantic proximity Read ↗

Crystal structure of DNA gyrase B' domain sheds lights on the mechanism for T-segment navigation.Semantic proximity Read ↗

Mutational analysis of Escherichia coli GreA protein reveals new functional activity independent of antipause and lethal when overexpressed.Semantic proximity Read ↗

Functional evaluation of four putative DNA-binding regions in Thermoanaerobacter tengcongensis reverse gyrase.Semantic proximity Read ↗

Mutation at the "exit gate" of the salmonella gyrase a subunit suppresses a defect in the gyrase B subunit.Semantic proximity Read ↗

Distinct regions of the Escherichia coli ParC C-terminal domain are required for substrate discrimination by topoisomerase IV.Semantic proximity Read ↗

Investigating the role of the latch in the positive supercoiling mechanism of reverse gyrase.Semantic proximity Read ↗

Targeted chromosomal Escherichia coli:dnaB exterior surface residues regulate DNA helicase behavior to maintain genomic stability and organismal fitness.Semantic proximity Read ↗

The reverse gyrase helicase-like domain is a nucleotide-dependent switch that is attenuated by the topoisomerase domain.Semantic proximity Read ↗

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