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 switch I and II regions of MinD are required for binding and activating MinC.

Journal of bacteriology - 1 Mar 2004

Zhou Huaijin, Lutkenhaus Joe

Abstract excerpt

MinD and MinC cooperate to form an efficient inhibitor of Z-ring formation that is spatially regulated by MinE. MinD activates MinC by recruiting it to the membrane and targeting it to a septal component. To better understand this activation, we have isolated loss-of-function mutations in minD and carried out site-directed mutagenesis. Many of these mutations block MinC-MinD interaction; however, they also...

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 Cell Membrane
Share to Cytoplasm

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

Share to Escherichia coli

Share to Escherichia coli Proteins

Share to Gene Expression Regulation, Bacterial

Share to Mutagenesis, Site-Directed

Share to Two-Hybrid System Techniques

Source

Open in PubMed Open full text

Identifiers

PMID: 14973039
DOI: 10.1128/JB.186.5.1546-1555.2004
PMCID: PMC344430

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 switch I and II regions of MinD are required for binding and activating MinC.PMID 14973039Read ↗

MinC mutants deficient in MinD- and DicB-mediated cell division inhibition due to loss of interaction with MinD, DicB, or a septal component.Semantic proximity Read ↗

MinE conformational dynamics regulate membrane binding, MinD interaction, and Min oscillation.Semantic proximity Read ↗

MinC and FtsZ mutant analysis provides insight into MinC/MinD-mediated Z ring disassembly.Semantic proximity Read ↗

New minC mutations suggest different interactions of the same region of division inhibitor MinC with proteins specific for minD and dicB coinhibition pathways.Semantic proximity Read ↗

Roles of MinC and MinD in the site-specific septation block mediated by the MinCDE system of Escherichia coli.Semantic proximity Read ↗

Direct MinE-membrane interaction contributes to the proper localization of MinDE in E. coli.Semantic proximity Read ↗

Mapping the MinE site involved in interaction with the MinD division site selection protein of Escherichia coli.Semantic proximity Read ↗

Proper placement of the Escherichia coli division site requires two functions that are associated with different domains of the MinE protein.Semantic proximity Read ↗

MinC/MinD copolymers are not required for Min function.Semantic proximity Read ↗

Division site placement in E.coli: mutations that prevent formation of the MinE ring lead to loss of the normal midcell arrest of growth of polar MinD membrane domains.Semantic proximity Read ↗

MinCD cell division proteins form alternating copolymeric cytomotive filaments.Semantic proximity Read ↗

Clostridial DivIVA and MinD interact in the absence of MinJ.Semantic proximity Read ↗

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