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

An amino-proximal domain required for the localization of FtsQ in the cytoplasmic membrane, and for its biological function in Escherichia coli.

Molecular microbiology - 1 Mar 1992

Dopazo A, Palacios P, Sánchez M, Pla J, Vicente M

Abstract excerpt

The location of FtsQ, an Escherichia coli protein essential for cell division, is, under physiological conditions, in the cytoplasmic membrane facing towards the periplasmic space. An amino-proximal hydrophobic domain is required for FtsQ to reach its location and for its activity in the cell. Overexpression of modified forms of FtsQ is deleterious for the cell.

Topics

Bacterial Proteins
Base Sequence
Biological Transport
Cell Division
Cell Membrane
Cloning, Molecular
Deoxyribonucleotides
Electrophoresis, Polyacrylamide Gel
Escherichia coli
Escherichia coli Proteins
Genetic Complementation Test

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Membrane Proteins

Molecular Sequence Data

Mutation

Plasmids

Trypsin

Source

Identifiers

PMID: 1574000
DOI: 10.1111/j.1365-2958.1992.tb01520.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1574000-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

An amino-proximal domain required for the localization of FtsQ in the cytoplasmic membrane, and for its biological function in Escherichia coli.PMID 1574000Read ↗

Membrane topology of the N-terminus of the Escherichia coli FtsK division protein.Semantic proximity Read ↗

Contribution of the FtsQ transmembrane segment to localization to the cell division site.Semantic proximity Read ↗

Analysis of ftsQ mutant alleles in Escherichia coli: complementation, septal localization, and recruitment of downstream cell division proteins.Semantic proximity Read ↗

Essential features of the pathway for protein translocation across the Escherichia coli cytoplasmic membrane.Semantic proximity Read ↗

Identification of essential arginine residues of Escherichia coli DedA/Tvp38 family membrane proteins YqjA and YghB.Semantic proximity Read ↗

Structural and mutational analysis of the cell division protein FtsQ.Semantic proximity Read ↗

Role of the carboxy terminus of Escherichia coli FtsA in self-interaction and cell division.Semantic proximity Read ↗

Temperature sensitivity and cell division defects in an Escherichia coli strain with mutations in yghB and yqjA, encoding related and conserved inner membrane proteins.Semantic proximity Read ↗

Genetic and functional analyses of the conserved C-terminal core domain of Escherichia coli FtsZ.Semantic proximity Read ↗

Sequence and length recognition of the C-terminal turnover element of LpxC, a soluble substrate of the membrane-bound FtsH protease.Semantic proximity Read ↗

Domain-swapping analysis of FtsI, FtsL, and FtsQ, bitopic membrane proteins essential for cell division in Escherichia coli.Semantic proximity Read ↗

YgbQ, a cell division protein in Escherichia coli and Vibrio cholerae, localizes in codependent fashion with FtsL to the division site.Semantic proximity Read ↗

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