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

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Article

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

The Journal of biological chemistry - 15 Feb 1992

Lewis M J, Simoni R D

Abstract excerpt

The a subunit is a membrane component of the F1F0-ATP synthase from Escherichia coli. Regions of a which appear important for membrane insertion or F0 assembly have been identified by analysis of both deletion mutants and fusion proteins which link the mutant a subunits to alkaline phosphatase. This analysis suggests the hydrophilic, amino-terminal domain of a is required for proper membrane targeting and/or...

Topics

Adenosine Triphosphate
Alkaline Phosphatase
Amino Acid Sequence
Cell Membrane
Chromosome Deletion
Escherichia coli
Genes, Bacterial
Genotype
Macromolecular Substances
Models, Structural
Molecular Sequence Data

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

NAD

Plasmids

Protein Conformation

Proton-Translocating ATPases

Recombinant Fusion Proteins

Spectrometry, Fluorescence

beta-Galactosidase

Source

Open in PubMed

Identifiers

PMID: 1531341

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1531341-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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