Chemotactic Transducer Proteins of Escherichia Coli Exhibit Homology with Methyl-accepting Proteins from Distantly Related Bacteria

Overview

Journal J Bacteriol

Publisher American Society for Microbiology

Specialty Microbiology

Date 1985 Jul 1

PMID 3924893

Citations 22

Authors

D M Nowlin

D O Nettleton

G W Ordal

G L Hazelbauer

Affiliations

Soon will be listed here.

Abstract

Transducers are transmembrane, methyl-accepting proteins central to the chemotactic systems of the enteric bacteria Escherichia coli and Salmonella typhimurium. Methyl-accepting proteins have been reported in a number of species in addition to these enteric bacteria. Those species include Bacillus subtilis and Spirochaeta aurantia, representatives of groups that diverged from ancestral enteric bacteria and from each other very early in bacterial evolution. An antiserum that reacts with all transducers of E. coli precipitated specifically methyl-accepting proteins from B. subtilis and S. aurantia, indicating that these proteins share antigenic determinants with transducers of E. coli. In addition, analysis of tryptic peptides by high-pressure liquid chromatography revealed similarities in the regions of methyl-accepting sites for proteins from all three species. These observations imply that structural features have been preserved in the three species from transducers contained in a common ancestor of eubacteria. It is thus reasonable to predict that other flagellated, chemotactic bacteria will be found to contain methyl-accepting proteins homologous to transducers of enteric bacteria.

Citing Articles

Substitutions in the periplasmic domain of low-abundance chemoreceptor trg that induce or reduce transmembrane signaling: kinase activation and context effects.

Beel B, Hazelbauer G J Bacteriol. 2001; 183(2):671-9.

PMID: 11133962 PMC: 94924. DOI: 10.1128/JB.183.2.671-679.2001.

Evolutionary conservation of methyl-accepting chemotaxis protein location in Bacteria and Archaea.

Gestwicki J, Lamanna A, Harshey R, McCarter L, Kiessling L, Adler J J Bacteriol. 2000; 182(22):6499-502.

PMID: 11053396 PMC: 94798. DOI: 10.1128/JB.182.22.6499-6502.2000.

Enhanced function conferred on low-abundance chemoreceptor Trg by a methyltransferase-docking site.

Feng X, Lilly A, Hazelbauer G J Bacteriol. 1999; 181(10):3164-71.

PMID: 10322018 PMC: 93772. DOI: 10.1128/JB.181.10.3164-3171.1999.

High- and low-abundance chemoreceptors in Escherichia coli: differential activities associated with closely related cytoplasmic domains.

Feng X, Baumgartner J, Hazelbauer G J Bacteriol. 1997; 179(21):6714-20.

PMID: 9352921 PMC: 179600. DOI: 10.1128/jb.179.21.6714-6720.1997.

Evidence for a methyl-accepting chemotaxis protein gene (mcp1) that encodes a putative sensory transducer in virulent Treponema pallidum.

Hagman K, Porcella S, Popova T, Norgard M Infect Immun. 1997; 65(5):1701-9.

PMID: 9125550 PMC: 175201. DOI: 10.1128/iai.65.5.1701-1709.1997.

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