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. 1984 Jun;81(11):3287–3291. doi: 10.1073/pnas.81.11.3287

Structure of the Trg protein: Homologies with and differences from other sensory transducers of Escherichia coli.

J Bollinger, C Park, S Harayama, G L Hazelbauer
PMCID: PMC345492  PMID: 6374654

Abstract

Transducer proteins are central to chemotaxis in Escherichia coli. Three transducer genes comprise a homologous gene family, while a fourth gene, trg, is more distantly related. We have determined the nucleotide sequence of trg. The deduced sequence of the Trg protein has features in common with other transducers as well as regions of significant divergence. The protein sequence suggests the same transmembrane structure postulated for other transducers: an extra cytoplasmic NH2-terminal domain connected by a membrane-spanning region to an intracellular COOH-terminal domain. The COOH-terminal domain of Trg exhibits substantial sequence identity with the corresponding domains of the other transducers, particularly near the sites of covalent modification. Trg appears to have the same five methyl-accepting sites identified in the Tsr protein. Two of those sites are glutamines that are deamidated to yield methyl-accepting glutamates, while the remainder are synthesized as glutamates. Conservation in number but not in position of modified glutamines in Trg compared to the other transducers is consistent with the notion that uncharged glutamines at a specific number of modification sites serve to balance the signaling state of newly synthesized transducers. The NH2-terminal domain of Trg exhibits no significant homology with other transducers, implying that trg may be a fusion of the common COOH-terminal transducer sequence with an unrelated NH2-terminal sequence. The location of specific mutations within trg provides support for the suggestion that ligand-binding sites are in the NH2-terminal domains.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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