Mutations in the MotA protein of Escherichia coli reveal domains critical for proton conduction.

doi:10.1016/0022-2836(91)90943-z

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

Back to search

Article

Mutations in the MotA protein of Escherichia coli reveal domains critical for proton conduction.

Journal of molecular biology - 20 Oct 1991

Blair D F, Berg H C

Abstract excerpt

The MotA protein of Escherichia coli is an essential component of the torque-generating units that drive the flagellar rotary motor. A variety of evidence indicates that MotA is involved in transmembrane proton conduction. We have now mapped a number of MotA mutants, focusing primarily on those previously shown to be dominant. Fifty-six mutations (all dominant), each causing severe or complete impairment of...

Topics

Alleles
Amino Acid Sequence
Bacterial Proteins
DNA Mutational Analysis
DNA-Directed RNA Polymerases
Electrophoresis, Polyacrylamide Gel
Endopeptidase K
Escherichia coli
Genes, Dominant
Ion Channels
Membrane Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Sequence Data

Mutation

Plasmids

Protons

Serine Endopeptidases

Spheroplasts

Viral Proteins

Source

Open in PubMed

Identifiers

PMID: 1719217
DOI: 10.1016/0022-2836(91)90943-z

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1719217-2026-08-29.1. 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.

discussions

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

Mutations in the MotA protein of Escherichia coli reveal domains critical for proton conduction.PMID 1719217Read ↗

Mutant MotB proteins in Escherichia coli.Semantic proximity Read ↗

The MotA protein of E. coli is a proton-conducting component of the flagellar motor.Semantic proximity Read ↗

Extragenic suppression of motA missense mutations of Escherichia coli.Semantic proximity Read ↗

Deletion analysis of MotA and MotB, components of the force-generating unit in the flagellar motor of Salmonella.Semantic proximity Read ↗

Tryptophan-scanning mutagenesis of MotB, an integral membrane protein essential for flagellar rotation in Escherichia coli.Semantic proximity Read ↗

Analysis of the motA flagellar motor gene from Rhodobacter sphaeroides, a bacterium with a unidirectional, stop-start flagellum.Semantic proximity Read ↗

Function of proline residues of MotA in torque generation by the flagellar motor of Escherichia coli.Semantic proximity Read ↗

Mot protein assembly into the bacterial flagellum: a model based on mutational analysis of the motB gene.Semantic proximity Read ↗

Flagellar movement driven by proton translocation.Semantic proximity Read ↗

Motility protein interactions in the bacterial flagellar motor.Semantic proximity Read ↗

Molecular and structural innovations of the stator motor complex at the dawn of flagellar motilitySemantic proximity Read ↗

Flagellar motility is mutagenic.Semantic proximity Read ↗

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