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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 attractant and repellent responses by modulating the activity of the cytoplasmic kinase CheA. In vivo intersubunit suppression...

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Identifiers

PMID: 8832891
DOI: 10.1126/science.274.5286.423

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

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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