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

Molecular architecture of the DNA-binding sites of the P-loop ATPases MipZ and ParA from Caulobacter crescentus.

Nucleic acids research - 21 May 2020

Corrales-Guerrero Laura, He Binbin, Refes Yacine, Panis Gaël, Bange Gert, Viollier Patrick H, Steinchen Wieland, Thanbichler Martin

Abstract excerpt

The spatiotemporal regulation of chromosome segregation and cell division in Caulobacter crescentus is mediated by two different P-loop ATPases, ParA and MipZ. Both of these proteins form dynamic concentration gradients that control the positioning of regulatory targets within the cell. Their proper localization depends on their nucleotide-dependent cycling between a monomeric and a dimeric state and on 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 Bacterial Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Binding Sites

Share to Caulobacter crescentus

Share to Diffusion

Share to DNA-Binding Proteins

Share to Protein Binding

Source

Open in PubMed Open full text

Identifiers

PMID: 32232335
DOI: 10.1093/nar/gkaa192
PMCID: PMC7229837

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

Molecular architecture of the DNA-binding sites of the P-loop ATPases MipZ and ParA from Caulobacter crescentus.PMID 32232335Read ↗

The CTPase activity of ParB determines the size and dynamics of prokaryotic DNA partition complexes.Semantic proximity Read ↗

A novel nucleoid-associated protein coordinates chromosome replication and chromosome partition.Semantic proximity Read ↗

A three-dimensional ParF meshwork assembles through the nucleoid to mediate plasmid segregation.Semantic proximity Read ↗

Bacillus subtilis ParB C-terminal lysine residues are essential for dimerization and in vivo function, indicating their roles in DNA sliding.Semantic proximity Read ↗

High-throughput identification of protein localization dependency networks.Semantic proximity Read ↗

Functional dichotomy and distinct nanoscale assemblies of a cell cycle-controlled bipolar zinc-finger regulator.Semantic proximity Read ↗

Soj (ParA) DNA binding is mediated by conserved arginines and is essential for plasmid segregation.Semantic proximity Read ↗

Probing the N-terminus of ParB using cysteine-scanning mutagenesis and thiol modification.Semantic proximity Read ↗

Uncoupling of nucleotide hydrolysis and polymerization in the ParA protein superfamily disrupts DNA segregation dynamics.Semantic proximity Read ↗

Multiple ParA/MinD ATPases coordinate the positioning of disparate cargos in a bacterial cellSemantic proximity Read ↗

Identification of the PhoB Regulon and Role of PhoU in the Phosphate Starvation Response of Caulobacter crescentus.Semantic proximity Read ↗

An SMC ATPase mutant disrupts chromosome segregation in Caulobacter.Semantic proximity Read ↗

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