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PMID: 337305 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Sensory transduction in Escherichia coli: role of a protein methylation reaction in sensory adaptation.

Goy MF, Springer MS, Adler J

Abstract

The behavioral response of Escherichia coli to the addition of a stimulatory compound is transient; thus the organism undergoes sensory adaptation. When the compound is removed, E. coli undergoes the inverse process, called deadaptation, and very rapidly regains its sensitivity to the stimulus. In this communication we demonstrate that the previously reported methylation of several cytoplasmic membrane proteins is correlated with, and very likely controls, the state of adaptation of the cell. In the absence of an added stimulus these proteins are methylated to a basal level. When the bacteria are stimulated by the addition of an attractant, the extent of methylation increases over a period of several minutes to a new level, which is maintained as long as the attractant is present. The magnitude of the increase in methylation is a function of the size of the stimulus and is directly proportional to the duration of the behavioral response. Upon removal of the attractant the level of methylation very rapidly falls to the basal value. Previously we have shown that adaptation requires methionine, but maintenance of the adapted state and de-adaptation do not [Springer, M. S., Goy, M. F. & Adler, J. (1975) Proc. Natl. Acad. Sci. USA 74, 183-187]; here we demonstrate that methylation requires methionine but maintenance of an attractant-induced level of methylation and the demethylation that occurs following removal of the attractant do not. These results strongly indicate a role for protein methylation in sensory adaptation.

MeSH Terms
Adaptation, Physiological Aminoisobutyric Acids/pharmacology Bacterial Proteins/metabolism,physiology Chemotaxis Electrophoresis, Polyacrylamide Gel Escherichia coli/physiology Fluorometry Kinetics Methylation Stimulation, Chemical
Chemicals
Aminoisobutyric Acids Bacterial Proteins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Goy M F
Springer M S
Adler J
References (18)
18 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1977-11-00
Pages
4964-8
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC432078
Subset
IM
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