PMID:15916610

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Citation

Li, M and Hazelbauer, GL (2005) Adaptational assistance in clusters of bacterial chemoreceptors. Mol. Microbiol. 56:1617-26

Abstract

Sensory adaptation of low-abundance chemoreceptors in Escherichia coli requires assistance from high-abundance receptors, because only high-abundance receptors carry the carboxyl-terminal pentapeptide sequence NWETF that enhances adaptational covalent modification. Using membrane vesicles containing both high-abundance receptor Tar and low-abundance receptor Trg, we observed effective assistance in vitro for all three adaptational modifications: methylation, demethylation and deamidation. These results demonstrated that adaptational assistance involves not only the previously documented assistance for methylation but also assistance for the two CheB-catalysed reactions. We determined rates of assisted methylation and demethylation at many ratios of assisting to assisted receptor. Analysis by a model of assistance indicated one Tar dimer could assist seven Trg dimers in methylation or five in demethylation, defining assistance neighbourhoods. These neighbourhoods were larger than a trimer of homodimers, required only receptors and were minimally affected by formation of signalling complexes. Time courses of assisted Trg methylation in membranes with low amounts of Tar showed that assisting receptors did not diffuse beyond initial neighbourhoods for at least two hours. Taken together, these observations indicate that chemoreceptors can form stable neighbourhoods larger than trimers in the absence of other chemotaxis proteins. Such interactions are likely to occur in natural receptor clusters in vivo.

Links

PubMed Online version:10.1111/j.1365-2958.2005.04641.x

Keywords

Adaptation, Physiological; Amino Acid Sequence; Bacterial Proteins/metabolism; Chemoreceptor Cells; Chemotaxis; Dimerization; Escherichia coli/physiology; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Membrane Proteins/chemistry; Membrane Proteins/metabolism; Methyltransferases/metabolism; Models, Biological; Molecular Sequence Data; Receptors, Cell Surface/chemistry; Receptors, Cell Surface/metabolism; Signal Transduction; Structure-Activity Relationship

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