| Literature DB >> 7007323 |
G L Hazelbauer, P Engström, S Harayama.
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.Entities:
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Year: 1981 PMID: 7007323 PMCID: PMC217242 DOI: 10.1128/jb.145.1.43-49.1981
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490