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The inner membrane histidine kinase EnvZ senses osmolality via helix-coil transitions in the cytoplasm
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The inner membrane histidine kinase EnvZ senses osmolality via helix-coil transitions in the cytoplasm
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Journal Article
The inner membrane histidine kinase EnvZ senses osmolality via helix-coil transitions in the cytoplasm
2012
Overview
Two‐component systems mediate bacterial signal transduction, employing a membrane sensor kinase and a cytoplasmic response regulator (RR). Environmental sensing is typically coupled to gene regulation. Understanding how input stimuli activate kinase autophosphorylation remains obscure. The EnvZ/OmpR system regulates expression of outer membrane proteins in response to osmotic stress. To identify EnvZ conformational changes associated with osmosensing, we used HDXMS to probe the effects of osmolytes (NaCl, sucrose) on the cytoplasmic domain of EnvZ (EnvZ
c
). Increasing osmolality decreased deuterium exchange localized to the four‐helix bundle containing the autophosphorylation site (His
243
). EnvZ
c
exists as an ensemble of multiple conformations and osmolytes favoured increased helicity. High osmolality increased autophosphorylation of His
243
, suggesting that these two events are linked.
In‐vivo
analysis showed that the cytoplasmic domain of EnvZ was sufficient for osmosensing, transmembrane domains were not required. Our results challenge existing claims of robustness in EnvZ/OmpR and support a model where osmolytes promote intrahelical H‐bonding enhancing helix stabilization, increasing autophosphorylation and downstream signalling. The model provides a conserved mechanism for signalling proteins that respond to diverse physical and mechanical stimuli.
The bacterial two‐component system EnvZ/OmpR governs the osmotic stress response. Increasing osmolality enhances intrahelical H‐bonding in the transmembrane kinase EnvZ, leading to helix stabilization, autophosphorylation and activation of downstream signalling.
Publisher
John Wiley & Sons, Ltd,Nature Publishing Group UK,Springer Nature B.V,Nature Publishing Group
Subject
amide hydrogen deuterium exchange mass spectrometry
/ Bacterial Outer Membrane Proteins - chemistry
/ Bacterial Outer Membrane Proteins - genetics
/ Bacterial Outer Membrane Proteins - physiology
/ EMBO20
/ EMBO37
/ Escherichia coli Proteins - chemistry
/ Escherichia coli Proteins - genetics
/ Escherichia coli Proteins - physiology
/ Kinases
/ Multienzyme Complexes - chemistry
/ Multienzyme Complexes - genetics
/ Multienzyme Complexes - physiology
/ Mutation
/ Protein Structure, Secondary - physiology
/ Proteins
/ Signal Transduction - physiology
