A topological analysis of subunit alpha from Escherichia coli F1F0-ATP synthase predicts eight transmembrane segments.

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

A topological analysis of subunit alpha from Escherichia coli F1F0-ATP synthase predicts eight transmembrane segments.

The Journal of biological chemistry - 25 Jun 1990

Lewis M J, Chang J A, Simoni R D

Abstract excerpt

The membrane topology of subunit alpha from the Escherichia coli F1F0-ATP synthase was studied using a gene fusion technique. Fusion proteins linking different amino-terminal fragments of the alpha subunit with an enzymatically active fragment of alkaline phosphatase were constructed by both random transposition of TnphoA and site-directed mutagenesis. Those proteins with high levels of alkaline phosphatase...

Topics

Alkaline Phosphatase
Amino Acid Sequence
Base Sequence
Cell Membrane
Cloning, Molecular
Codon
DNA Transposable Elements
Escherichia coli
Genotype
Macromolecular Substances
Models, Structural

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Sequence Data

Mutation

Plasmids

Protein Conformation

Proton-Translocating ATPases

Recombinant Fusion Proteins

Source

Open in PubMed

Identifiers

PMID: 2162353

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2162353-2026-08-29.1. 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

A topological analysis of subunit alpha from Escherichia coli F1F0-ATP synthase predicts eight transmembrane segments.PMID 2162353Read ↗

Deletions in hydrophilic domains of subunit a from the Escherichia coli F1F0-ATP synthase interfere with membrane insertion or F0 assembly.Semantic proximity Read ↗

Functional analysis of membranous Fo-a subunit of F1Fo-ATP synthase by in vitro protein synthesis.Semantic proximity Read ↗

Lengthening the second stalk of F(1)F(0) ATP synthase in Escherichia coli.Semantic proximity Read ↗

The ATP synthase of Escherichia coli: structure and function of F(0) subunits.Semantic proximity Read ↗

Time-delayed in vivo assembly of subunit a into preformed Escherichia coli FoF1 ATP synthase.Semantic proximity Read ↗

Insights into the regulatory function of the ɛ subunit from bacterial F-type ATP synthases: a comparison of structural, biochemical and biophysical data.Semantic proximity Read ↗

Site-directed mutagenesis of the conserved beta subunit tyrosine 331 of Escherichia coli ATP synthase yields catalytically active enzymes.Semantic proximity Read ↗

Subunit δ is the key player for assembly of the H(+)-translocating unit of Escherichia coli F(O)F1 ATP synthase.Semantic proximity Read ↗

Crystal structure of the epsilon subunit of the proton-translocating ATP synthase from Escherichia coli.Semantic proximity Read ↗

Structure of the membrane domain of subunit b of the Escherichia coli F0F1 ATP synthase.Semantic proximity Read ↗

On the role of Arg-210 and Glu-219 of subunit a in proton translocation by the Escherichia coli F0F1-ATP synthase.Semantic proximity Read ↗

The P-Type ATPase SuperfamilySemantic proximity Read ↗

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