Document Detail

Reversible receptor methylation is essential for normal chemotaxis of Escherichia coli in gradients of aspartic acid.
MedLine Citation:
PMID:  2829179     Owner:  NLM     Status:  MEDLINE    
The chemotaxis of wild-type cells of Escherichia coli and double mutants lacking the methyltransferase and the methylesterase activities of the receptor modification system has been compared in spatial gradients of aspartic acid. Previous studies showing that a chemotactic response can be observed for the mutant raised questions about the role of methylation in the bacterial memory. To clarify the role of methylation, the redistribution of bacteria in stabilized defined gradients of aspartic acid was monitored by light scattering. There was no redistribution of the mutant cells in nonsaturating gradients of aspartic acid, but over the same range these mutant bacteria were observed to respond and to adapt during tethering experiments. In large saturating gradients of aspartate, slight movement of the mutant up the gradient was observed. These results show that dynamic receptor methylation is required for the chemotactic response to gentle gradients of aspartic acid and that methylation resets to zero and is part of the normal wild-type memory. There are certain gradients, however, in which the methylation-deficient mutants show chemotactic ability, thus explaining the apparent anomaly.
R M Weis; D E Koshland
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Proceedings of the National Academy of Sciences of the United States of America     Volume:  85     ISSN:  0027-8424     ISO Abbreviation:  Proc. Natl. Acad. Sci. U.S.A.     Publication Date:  1988 Jan 
Date Detail:
Created Date:  1988-03-02     Completed Date:  1988-03-02     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  83-7     Citation Subset:  IM    
Department of Biochemistry, University of California, Berkeley 94720.
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MeSH Terms
Aspartic Acid / metabolism*
Cell Movement
Escherichia coli / enzymology,  genetics,  physiology*
Methyltransferases / metabolism*
Receptors, Amino Acid*
Receptors, Cell Surface / metabolism*
Grant Support
Reg. No./Substance:
0/Receptors, Amino Acid; 0/Receptors, Cell Surface; 0/aspartic acid receptor; 56-84-8/Aspartic Acid; EC 2.1.1.-/Methyltransferases; EC 2.1.1.-/chemotaxis methyltransferase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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