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Methyl-accepting chemotaxis protein III and transducer gene trg
Author(s) -
Gerald L. Hazelbauer,
P. Engström,
Shigeaki Harayama
Publication year - 1981
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.145.1.43-49.1981
Subject(s) - chemotaxis , biology , gene product , gel electrophoresis , membrane protein , polyacrylamide gel electrophoresis , mutant , gene , escherichia coli , biochemistry , microbiology and biotechnology , membrane , gene expression , enzyme , receptor
A comparison of the two-dimensional gel patterns of methyl-3H- and 35S-labeled membrane proteins from trg+ and trg null mutant strains of Escherichia coli indicated that the product of trg is probably methyl-accepting chemotaxis protein III. Like the other known methyl-accepting chemotaxis proteins, the trg product is a membrane protein that migrates as more than one species in sodium dodecyl sulfate-polyacrylamide gel electrophoresis, implying that it too is multiple methylated. It appears likely that all chemoreceptors are linked to the tumble regulator through a single class of membrane protein transducers which are methyl-accepting proteins. Three transducers are coded for by genes tsr, tar, and, probably, trg. Another methyl-accepting protein, which is not related to any of these genes, was observed.

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