title: Methyl-accepting chemotaxis protein III and transducer gene trg.
abstract: 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.
mesh_terms: D001426:Bacterial Proteins / Q000032:analysis / Q000235:genetics*; D002630:Chemotactic Factors / Q000032:analysis / Q000235:genetics*; D002633:Chemotaxis; D004926:Escherichia coli / Q000235:genetics* / Q000502:physiology; D005796:Genes; D008565:Membrane Proteins / Q000032:analysis / Q000235:genetics*; D000072236:Methyl-Accepting Chemotaxis Proteins; D008745:Methylation; D009154:Mutation
chemical_list: D001426:Bacterial Proteins; D002630:Chemotactic Factors; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins; C000607604:tsr protein, E coli