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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1977 Nov;74(11):4964–4968. doi: 10.1073/pnas.74.11.4964

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

Michael F Goy *,, Martin S Springer ‡,‡,, Julius Adler ‡,
PMCID: PMC432078  PMID: 337305

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.

Keywords: bacterial chemotaxis, protein modification, electrophoresis

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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