Clustering of the chemoreceptor complex in Escherichia coli is independent of the methyltransferase CheR and the methylesterase CheB.
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.
Lybarger
S R
SR
Department of Biology, University of Michigan, Ann Arbor, Michigan 48109-1048, USA.
Maddock
J R
JR
D001426:Bacterial Proteins / Q000378:metabolism*; D002265:Carboxylic Ester Hydrolases / Q000235:genetics / Q000502:physiology*; D002628:Chemoreceptor Cells / Q000378:metabolism*; D002633:Chemotaxis; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D029968:Escherichia coli Proteins; D017353:Gene Deletion; D000071677:Histidine Kinase; D008565:Membrane Proteins / Q000378:metabolism*; D000072236:Methyl-Accepting Chemotaxis Proteins; D008780:Methyltransferases / Q000235:genetics / Q000502:physiology*
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins; D008780:Methyltransferases; C038706:chemotaxis methyltransferase; D000071677:Histidine Kinase; C000607608:cheA protein, E coli; D002265:Carboxylic Ester Hydrolases; C041144:chemotactic protein methylesterase