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PMID: 10464232 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Clustering of the chemoreceptor complex in Escherichia coli is independent of the methyltransferase CheR and the methylesterase CheB.

Journal of bacteriology ·Vol. 181 ·No. 17 ·1999-09-00 ·Pages 5527-9

Lybarger SR, Maddock JR

Abstract

The Escherichia coli chemoreceptors and their associated cytoplasmic proteins, CheA and CheW, cluster predominantly at the cell poles. The nature of the clustering remains a mystery. Recent studies suggest that CheR binding to and/or methylation of the chemoreceptors may play a role in chemoreceptor complex aggregation. In this study, we examined the intracellular distribution of the chemoreceptors by immunoelectron microscopy in strains lacking either the methyltransferase CheR or the methylesterase CheB. The localization data revealed that, in vivo, aggregation of the chemoreceptor complex was independent of either CheR or CheB.

MeSH Terms
Bacterial Proteins/metabolism Carboxylic Ester Hydrolases/genetics,physiology Chemoreceptor Cells/metabolism Chemotaxis Escherichia coli/enzymology,genetics Escherichia coli Proteins Gene Deletion Histidine Kinase Membrane Proteins/metabolism Methyl-Accepting Chemotaxis Proteins Methyltransferases/genetics,physiology
Chemicals
Bacterial Proteins Escherichia coli Proteins Membrane Proteins Methyl-Accepting Chemotaxis Proteins Methyltransferases chemotaxis methyltransferase Histidine Kinase cheA protein, E coli Carboxylic Ester Hydrolases chemotactic protein methylesterase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Lybarger S R
Department of Biology, University of Michigan, Ann Arbor, Michigan 48109-1048, USA.
Maddock J R
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1999-09-00
Pages
5527-9
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC94067
Subset
IM
Grants
NIGMS NIH HHS · R01 GM055133 · United States
NIGMS NIH HHS · GM-55133 · United States
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