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

SpoIIIE protein achieves directional DNA translocation through allosteric regulation of ATPase activity by an accessory domain.

The Journal of biological chemistry - 4 Oct 2013

Besprozvannaya Marina, Pivorunas Valerie L, Feldman Zachary, Burton Briana M

Abstract excerpt

Bacterial chromosome segregation utilizes highly conserved directional translocases of the SpoIIIE/FtsK family. These proteins employ an accessory DNA-binding domain (γ) to dictate directionality of DNA transport. It remains unclear how the interaction of γ with specific recognition sequences coordinates directional DNA translocation. We demonstrate that the γ domain of SpoIIIE inhibits ATPase activity of the...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphatases
Share to Allosteric Regulation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Amino Acid Motifs

Share to Bacillus subtilis

Share to Biological Transport

Share to DNA, Bacterial

Share to Protein Subunits

Share to Structure-Activity Relationship

Source

Open in PubMed Open full text

Identifiers

PMID: 23974211
DOI: 10.1074/jbc.M113.484055
PMCID: PMC3789994

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

SpoIIIE protein achieves directional DNA translocation through allosteric regulation of ATPase activity by an accessory domain.PMID 23974211Read ↗

Mechanistic study of classical translocation-dead SpoIIIE36 reveals the functional importance of the hinge within the SpoIIIE motor.Semantic proximity Read ↗

The ATPase SpoIIIE transports DNA across fused septal membranes during sporulation in Bacillus subtilis.Semantic proximity Read ↗

Separating speed and ability to displace roadblocks during DNA translocation by FtsK.Semantic proximity Read ↗

Spo0J regulates the oligomeric state of Soj to trigger its switch from an activator to an inhibitor of DNA replication initiation.Semantic proximity Read ↗

Bacillus subtilis SpoIIIE protein required for DNA segregation during asymmetric cell division.Semantic proximity Read ↗

Evidence that the SpoIIIE DNA translocase participates in membrane fusion during cytokinesis and engulfment.Semantic proximity Read ↗

Allosteric communication between signal peptides and the SecA protein DEAD motor ATPase domain.Semantic proximity Read ↗

Acyl carrier protein promotes MukBEF action in Escherichia coli chromosome organization-segregation.Semantic proximity Read ↗

Directional motility of kinesin motor proteins.Semantic proximity Read ↗

Global co-ordination of protein translocation by the SecA IRA1 switch.Semantic proximity Read ↗

Accessory factors determine the order of strand exchange in Xer recombination at psi.Semantic proximity Read ↗

Dynamic movement of the ParA-like Soj protein of B. subtilis and its dual role in nucleoid organization and developmental regulation.Semantic proximity Read ↗

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