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
Related Documents :
9721759 - Elevated "hydroxyl radical" generation in vivo in an animal model of amyotrophic latera...
4066609 - Fatty aldehyde dehydrogenases in acinetobacter sp. strain ho1-n: role in hexadecanol me...
127619 - Isolation and characterization of a mutant of neurospora crassa deficient in general am...
21944859 - Synthesis and properties of novel 2'-o-alkoxymethyl-modified nucleic acids.
20722419 - Contribution of amino acid region 659-663 of factor va heavy chain to the activity of f...
8000539 - Fatty acid biosynthesis in novel ufa mutants of neurospora crassa.
7085639 - Purification and macromolecular properties of a sialic acid-specific lectin from the sl...
5056669 - The amino acid sequence of a major nonimmunoglobulin component of some amyloid fibrils.
9599269 - Two new cembranoids from croton oblongifolius
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.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
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

Previous Document:  Structural alteration in the MYB protooncogene and deletion within the gene encoding alpha-type prot...
Next Document:  Sequence requirements for cleavage activation of influenza virus hemagglutinin expressed in mammalia...