Bacterial chemotaxis coupling protein: Structure, function and diversity

Abstract

In most signal transduction systems, coupling or scaffold proteins establish crucial connections between receptors and histidine kinases. These connections are important for signal transduction. The bacterial chemotaxis system is a canonical signal transduction system that relies on coupling proteins. The coupling proteins in the chemotaxis system have two architectures: CheW or CheV. In a typical chemotaxis signal transduction system, two CheW coupling protein molecules bridge a histidine kinase CheA dimer and two chemoreceptor (also called as methyl-accepting chemotaxis protein, MCP) trimers of dimers to form a core signaling complex and couple CheA activity to chemoreceptor control. Although CheW is a small cytoplasmic protein, it plays multiple functions in chemotaxis. CheW also builds connections between core signaling complexes, which leads to the formation of large chemosensory arrays that are responsible for collecting and amplifying signals from various chemoreceptors. Another coupling protein, CheV, shares a largely redundant ability with CheW; however, the function of CheV is not identical to that of CheW in chemotaxis. In this article, we summarize the molecular mechanism of chemotaxis in Escherichia coli and review the recent advances in the structural details and functions of CheW and CheV. Furthermore, we focus on the diversity of coupling proteins and discuss the relationship among multiple coupling proteins in one organism.

Keywords: Chemoreceptor; Core signaling complex; Protein interaction; Protein phosphorylation; Signal transduction.