Regulatory Role of an Interdomain Linker in the Bacterial Chemotaxis Histidine Kinase CheA

Journal of Bacteriology
Xueye DingXiqing Wang

Abstract

The histidine kinase CheA plays a central role in signal integration, conversion, and amplification in the bacterial chemotaxis signal transduction pathway. The kinase activity is regulated in chemotaxis signaling complexes formed via the interactions among CheA's regulatory domain (P5), the coupling protein CheW, and transmembrane chemoreceptors. Despite recent advancements in the understanding of the architecture of the signaling complex, the molecular mechanism underlying this regulation remains elusive. An interdomain linker that connects the catalytic (P4) and regulatory domains of CheA may mediate regulatory signals from the P5-CheW-receptor interactions to the catalytic domain. To investigate whether this interdomain linker is capable of both activating and inhibiting CheA, we performed in vivo screens to search for P4-P5 linker mutations that result in different CheA autokinase activities. Several CheA variants were identified with kinase activities ranging from 30% to 670% of the activity of wild-type CheA. All of these CheA variants were defective in receptor-mediated kinase activation, indicating that the natural receptor-mediated signal transmission pathway was simultaneously affected by these mutations. The altered...Continue Reading

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Citations

Sep 11, 2019·Journal of Bacteriology·Germán E Piñas, John S Parkinson
Jul 2, 2020·Nucleic Acids Research·Maria TauberWolfgang Fischle
Jul 19, 2019·Proceedings of the National Academy of Sciences of the United States of America·Qun GaoJohn S Parkinson
Nov 12, 2020·Science Signaling·Alise R MuokBrian R Crane

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