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
Bacterial Proteins/analysis,genetics
Chemotactic Factors/analysis,genetics
Chemotaxis
Escherichia coli/genetics,physiology
Genes
Membrane Proteins/analysis,genetics
Methyl-Accepting Chemotaxis Proteins
Methylation
Mutation
Chemicals
Bacterial Proteins
Chemotactic Factors
Membrane Proteins
Methyl-Accepting Chemotaxis Proteins
tsr protein, E coli
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Hazelbauer G L
Engström P
Harayama S
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31 references, click to expand
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