Signaling by the Escherichia coli aspartate chemoreceptor Tar with a single cytoplasmic domain per dimer.

doi:10.1126/science.274.5286.423

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Article

Signaling by the Escherichia coli aspartate chemoreceptor Tar with a single cytoplasmic domain per dimer.

Science (New York, N.Y.) - 18 Oct 1996

Tatsuno I, Homma M, Oosawa K, Kawagishi I

Abstract excerpt

Many transmembrane receptors are oligomeric proteins. Binding of a ligand may alter the oligomeric state of the receptor, induce structural changes within the oligomer, or both. The bacterial aspartate chemoreceptor Tar forms a homodimer in the presence or absence of ligands. Tar mediates attract...

Topics

Aspartic Acid
Bacterial Proteins
Chemoreceptor Cells
Chemotaxis
Cytoplasm
Dimerization
Escherichia coli
Escherichia coli Proteins
Glycerol
Histidine Kinase
Membrane Proteins
Methyl-Accepting Chemotaxis Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Methylation

Mutation

Protein Conformation

Protein Kinases

Receptors, Cell Surface

Signal Transduction

Source

Open in PubMed

Identifiers

PMID: 8832891
DOI: 10.1126/science.274.5286.423

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8832891-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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Signaling by the Escherichia coli aspartate chemoreceptor Tar with a single cytoplasmic domain per dimer.PMID 8832891Read ↗

Attractant signaling by an aspartate chemoreceptor dimer with a single cytoplasmic domain.Semantic proximity Read ↗

Conformational suppression of inter-receptor signaling defects.Semantic proximity Read ↗

Maltose-binding protein interacts simultaneously and asymmetrically with both subunits of the Tar chemoreceptor.Semantic proximity Read ↗

Intersubunit interaction between transmembrane helices of the bacterial aspartate chemoreceptor homodimer.Semantic proximity Read ↗

Mutational analysis of N381, a key trimer contact residue in Tsr, the Escherichia coli serine chemoreceptor.Semantic proximity Read ↗

Transmembrane signalling by the chimeric chemosensory receptors of Escherichia coli Tsr and Tar with heterologous membrane-spanning regions.Semantic proximity Read ↗

Residues at the cytoplasmic end of transmembrane helix 2 determine the signal output of the TarEc chemoreceptor.Semantic proximity Read ↗

Ligand specificity determined by differentially arranged common ligand-binding residues in bacterial amino acid chemoreceptors Tsr and Tar.Semantic proximity Read ↗

Arginine mutations within a transmembrane domain of Tar, an Escherichia coli aspartate receptor, can drive homodimer dissociation and heterodimer association in vivo.Semantic proximity Read ↗

Different signaling roles of two conserved residues in the cytoplasmic hairpin tip of Tsr, the Escherichia coli serine chemoreceptor.Semantic proximity Read ↗

Inversion of thermosensing property of the bacterial receptor Tar by mutations in the second transmembrane region.Semantic proximity Read ↗

Role of threonine residue 154 in ligand recognition of the tar chemoreceptor in Escherichia coli.Semantic proximity Read ↗

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