Literature DB >> 7045096

Ordered methylation of the methyl-accepting chemotaxis proteins of Escherichia coli.

M S Springer, B Zanolari, P A Pierzchala.   

Abstract

The methylation of glutamic acid residues on 3 membrane proteins, MCPI, MCPII, and MCPIII, plays an essential role in the chemotactic response of Escherichia coli. In the absence of a chemotactic stimulus the methyl-accepting chemotaxis proteins (MCPs) are methylated to a basal level. This level rises to a new plateau when an attractant is added and then falls to its original basal value when the attractant is removed. We have now been able to show that the properties of the glutamic acid residues which become methylated after stimulation with an attractant differ from the properties of the residues methylated on the basal level. Our data imply that there is a preferred order in which those residues are methylated and demethylated.

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Year:  1982        PMID: 7045096

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  4 in total

1.  A model of excitation and adaptation in bacterial chemotaxis.

Authors:  P A Spiro; J S Parkinson; H G Othmer
Journal:  Proc Natl Acad Sci U S A       Date:  1997-07-08       Impact factor: 11.205

Review 2.  Protein phosphorylation and regulation of adaptive responses in bacteria.

Authors:  J B Stock; A J Ninfa; A M Stock
Journal:  Microbiol Rev       Date:  1989-12

3.  Solubilization of a vectorial transmembrane receptor in functional form: aspartate receptor of chemotaxis.

Authors:  E Bogonez; D E Koshland
Journal:  Proc Natl Acad Sci U S A       Date:  1985-08       Impact factor: 11.205

4.  Sensory transduction in Escherichia coli: regulation of the demethylation rate by the CheA protein.

Authors:  M S Springer; B Zanolari
Journal:  Proc Natl Acad Sci U S A       Date:  1984-08       Impact factor: 11.205

  4 in total

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