Transmembrane Signal Transduction in Two‐Component Systems: Piston, Scissoring, or Helical Rotation?

Allosteric and transmembrane (TM) signaling are among the major questions of structural biology. Here, we review and discuss signal transduction in four‐helical TM bundles, focusing on histidine kinases and chemoreceptors found in two‐component systems. Previously, piston, scissors, and helical rota...

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Bibliographic Details
Published in:BioEssays 2018-02, Vol.40 (2), p.n/a
Main Authors: Gushchin, Ivan, Gordeliy, Valentin
Format: Article
Language:English
Subjects:
Allosteric properties
Archaeal Proteins - chemistry
Carotenoids - chemistry
Cell Membrane - chemistry
chemoreceptor
Chemoreceptors
coiled coil
Crystal structure
Crystallography
Cutting tools
Escherichia coli Proteins - chemistry
HAMP domain
Helices
Histidine
Histidine kinase
Histidine Kinase - chemistry
Kinases
Membrane Proteins - chemistry
membrane receptors
Phosphoproteins - chemistry
Phototaxis
Protein Domains
Protein Structure, Quaternary
Protein Structure, Secondary
Signal Transduction
Signaling
transmembrane signaling
two‐component signaling systems
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Summary:Allosteric and transmembrane (TM) signaling are among the major questions of structural biology. Here, we review and discuss signal transduction in four‐helical TM bundles, focusing on histidine kinases and chemoreceptors found in two‐component systems. Previously, piston, scissors, and helical rotation have been proposed as the mechanisms of TM signaling. We discuss theoretically possible conformational changes and examine the available experimental data, including the recent crystallographic structures of nitrate/nitrite sensor histidine kinase NarQ and phototaxis system NpSRII:NpHtrII. We show that TM helices can flex at multiple points and argue that the various conformational changes are not mutually exclusive, and often are observed concomitantly, throughout the TM domain or in its part. The piston and scissoring motions are the most prominent motions in the structures, but more research is needed for definitive conclusions. Models of allosteric transmembrane (TM) signaling in microbial sensor histidine kinases and chemoreceptors are discussed in light of recent crystallographic structures. It is shown that the TM α‐helices are flexible and various conformational changes are often observed concomitantly. The piston and scissoring motions are the most prominent in the structures.
ISSN:0265-9247
1521-1878
DOI:10.1002/bies.201700197