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PMID: 9473056 Published · ppublish English 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.

Both acetate kinase and acetyl coenzyme A synthetase are involved in acetate-stimulated change in the direction of flagellar rotation in Escherichia coli.

Journal of bacteriology ·Vol. 180 ·No. 4 ·1998-02-00 ·Pages 985-8

Barak R, Abouhamad WN, Eisenbach M

Abstract

Escherichia coli strains overproducing the response regulator CheY respond to acetate by increasing their clockwise bias of flagellar rotation, even when they lack other chemotaxis proteins. With acetate metabolism mutants, we demonstrate that both acetate kinase and acetyl coenzyme A synthetase are involved in this response. Thus, a response was observed when one of these enzymes was missing but not when both were absent.

MeSH Terms
Acetate Kinase/metabolism Acetate-CoA Ligase/metabolism Acetates/pharmacology Bacterial Proteins Chemotaxis/physiology Escherichia coli/drug effects,physiology Escherichia coli Proteins Flagella/drug effects Membrane Proteins/genetics,metabolism Methyl-Accepting Chemotaxis Proteins Movement Mutation Recombinant Proteins/metabolism Signal Transduction
Chemicals
Acetates Bacterial Proteins Escherichia coli Proteins Membrane Proteins Methyl-Accepting Chemotaxis Proteins Recombinant Proteins cheY protein, E coli Acetate Kinase Acetate-CoA Ligase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Barak R
Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot, Israel.
Abouhamad W N
Eisenbach M
References (18)
18 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1998-02-00
Pages
985-8
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC106981
Subset
IM
Grants
NIGMS NIH HHS · R01 GM050860 · United States
NIGMS NIH HHS · GM50860 · United States
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