Research ArticleStructural Biology

Specificity of the CheR2 Methyltransferase in Pseudomonas aeruginosa Is Directed by a C-Terminal Pentapeptide in the McpB Chemoreceptor

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Science Signaling  08 Apr 2014:
Vol. 7, Issue 320, pp. ra34
DOI: 10.1126/scisignal.2004849

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Guided by a Pentapeptide

Sensory adaptation is critical to chemotaxis and survival in bacteria. The chemosensory response is modified by reversible methylation of the cytoplasmic domain of the chemoreceptor. Some chemoreceptors have a pentapeptide sequence at the C terminus, which can bind the methyltransferases or methylesterases, increasing their local concentration. García-Fontana et al. investigated the selectivity of the interactions between the methyltransferases of the CheR family and chemoreceptors in Pseudomonas aeruginosa. Of the four methyltransferases and 26 chemoreceptors, a functional interaction (binding and methylation) was only detected between CheR2 and the chemoreceptor McpB (methyl-accepting chemotaxis protein B), which has the pentapeptide GWEEF at its C terminus. Both the physical and functional interactions between CheR2 and McpB were abolished by deletion of either GWEEF in McpB or a tripeptide motif in CheR2, which was partially conserved in pentapeptide-binding CheRs in other bacteria species. The findings identify a specificity mechanism in the functional modification of bacterial chemoreceptors.