Issue 5, 2011

Receptor domains of two-component signal transduction systems

Abstract

Two-component signal transduction systems are found ubiquitously in prokaryotes, and in archaea, fungi, yeast and some plants, where they regulate physiologic and molecular processes at both transcriptional and post-transcriptional levels. Two-component systems sense changes in environmental conditions when a specific ligand binds to the receptor domain of the histidine kinase sensory component. The structures of many histidine kinase receptors are known, including those which sense extracellular and cytoplasmic signals. In this review, we discuss the basic architecture of two-component signalling circuits, including known system ligands, structure and function of both receptor and signalling domains, the chemistry of phosphotransfer, and cross-talk between different two-component pathways. Given the importance of these systems in regulating cellular responses, many biochemical techniques have been developed for their study and analysis. We therefore also review current methods used to study two-component signalling, including a new affinity-based proteomics approach used to study inducible resistance to the antibiotic vancomycin through the VanSR two-component signal transduction system.

Graphical abstract: Receptor domains of two-component signal transduction systems

Article information

Article type
Review Article
Submitted
13 Dec 2010
Accepted
31 Jan 2011
First published
24 Feb 2011

Mol. BioSyst., 2011,7, 1388-1398

Receptor domains of two-component signal transduction systems

J. Perry, K. Koteva and G. Wright, Mol. BioSyst., 2011, 7, 1388 DOI: 10.1039/C0MB00329H

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