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

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

Nucleic acids research - 24 Feb 2026

Aleshintsev Aleksey, Way Lindsey E, Lai Ngoc Khanh, Guerra Bianca, Dorantes Paloma, Serwaa Lois Akosua, Anulao Sealtiel, Molina Miranda, Wang Xindan, Kim HyeongJun

Abstract excerpt

The broadly conserved ParB protein performs crucial functions in bacterial chromosome segregation and replication regulation. The cellular function of ParB requires it to dimerize, recognize parS DNA sequences, clamp on DNA, then slide to adjacent sequences through nonspecific DNA binding. How ParB coordinates nonspecific DNA binding and sliding remains elusive. Here, we combine multiple in vitro biophysical and...

Read the complete abstract on PubMed

Topics

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

Share to Bacillus subtilis
Share to Bacterial Proteins

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

Share to DNA, Bacterial

Share to DNA-Binding Proteins

Share to Lysine

Share to Models, Molecular

Share to Protein Domains

Share to Protein Multimerization

Source

Open in PubMed Open full text

Identifiers

PMID: 41830326
DOI: 10.1093/nar/gkag202
PMCID: PMC12988329

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 23 Oct 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

Bacillus subtilis ParB C-terminal lysine residues are essential for dimerization and in vivo function, indicating their roles in DNA sliding.PMID 41830326Read ↗

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

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

Deacetylation enhances ParB–DNA interactions affecting chromosome segregation in Streptomyces coelicolorSemantic proximity Read ↗

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

The ParB- parS Chromosome Segregation System Modulates Competence Development in Streptococcus pneumoniaeSemantic proximity Read ↗

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

Dissection of the ATPase active site of P1 ParA reveals multiple active forms essential for plasmid partition.Semantic proximity Read ↗

Diversification of DNA-Binding Specificity by Permissive and Specificity-Switching Mutations in the ParB/Noc Protein Family.Semantic proximity Read ↗

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

A single parS sequence from the cluster of four sites closest to oriC is necessary and sufficient for proper chromosome segregation in Pseudomonas aeruginosa.Semantic proximity Read ↗

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

Cryptic adaptor protein interactions regulate DNA replication initiationSemantic proximity Read ↗

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