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Paradoxical enhancement of chemoreceptor detection sensitivity by a sensory adaptation enzyme.


ABSTRACT: A sensory adaptation system that tunes chemoreceptor sensitivity enables motile Escherichia coli cells to track chemical gradients with high sensitivity over a wide dynamic range. Sensory adaptation involves feedback control of covalent receptor modifications by two enzymes: CheR, a methyltransferase, and CheB, a methylesterase. This study describes a CheR function that opposes the signaling consequences of its catalytic activity. In the presence of CheR, a variety of mutant serine chemoreceptors displayed up to 40-fold enhanced detection sensitivity to chemoeffector stimuli. This response enhancement effect did not require the known catalytic activity of CheR, but did involve a binding interaction between CheR and receptor molecules. Response enhancement was maximal at low CheR:receptor stoichiometry and quantitative analyses argued against a reversible binding interaction that simply shifts the ON-OFF equilibrium of receptor signaling complexes. Rather, a short-lived CheR binding interaction appears to promote a long-lasting change in receptor molecules, either a covalent modification or conformation that enhances their response to attractant ligands.

SUBMITTER: Lai RZ 

PROVIDER: S-EPMC5594695 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature

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Paradoxical enhancement of chemoreceptor detection sensitivity by a sensory adaptation enzyme.

Lai Run-Zhi RZ   Han Xue-Sheng XS   Dahlquist Frederick W FW   Parkinson John S JS  

Proceedings of the National Academy of Sciences of the United States of America 20170821 36


A sensory adaptation system that tunes chemoreceptor sensitivity enables motile <i>Escherichia coli</i> cells to track chemical gradients with high sensitivity over a wide dynamic range. Sensory adaptation involves feedback control of covalent receptor modifications by two enzymes: CheR, a methyltransferase, and CheB, a methylesterase. This study describes a CheR function that opposes the signaling consequences of its catalytic activity. In the presence of CheR, a variety of mutant serine chemor  ...[more]

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