Dynamic domain arrangement of CheA-CheY complex regulates bacterial thermotaxis, as revealed by NMR.
Sci Rep. 2017 Nov 28;7(1):16462
Authors: Minato Y, Ueda T, Machiyama A, Iwaï H, Shimada I
Abstract
Bacteria utilize thermotaxis signal transduction proteins, including CheA, and CheY, to switch the direction of the cell movement. However, the thermally responsive machinery enabling warm-seeking behavior has not been identified. Here we examined the effects of temperature on the structure and dynamics of the full-length CheA and CheY complex, by NMR. Our studies revealed that the CheA-CheY complex exists in equilibrium between multiple states, including one state that is preferable for the autophosphorylation of CheA, and another state that is preferable for the phosphotransfer from CheA to CheY. With increasing temperature, the equilibrium shifts toward the latter state. The temperature-dependent population shift of the dynamic domain arrangement of the CheA-CheY complex induced changes in the concentrations of phosphorylated CheY that are comparable to those induced by chemical attractants or repellents. Therefore, the dynamic domain arrangement of the CheA-CheY complex functions as the primary thermally responsive machinery in warm-seeking behavior.
[NMR paper] Contrasting roles of dynamics in protein allostery: NMR and structural studies of CheY and the third PDZ domain from PSD-95.
Contrasting roles of dynamics in protein allostery: NMR and structural studies of CheY and the third PDZ domain from PSD-95.
Related Articles Contrasting roles of dynamics in protein allostery: NMR and structural studies of CheY and the third PDZ domain from PSD-95.
Biophys Rev. 2015 Jun;7(2):217-226
Authors: Lee AL
Abstract
Allosteric regulation is a ubiquitous phenomenon exploited in biological processes to control cells in a myriad of ways. It is also of emerging interest in the design of functional proteins and therapeutics....
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Universal Stress Protein Regulates Electron Transferand Superoxide Generation Activities of the Cytochrome bc1 Complex from Rhodobacter sphaeroides
Universal Stress Protein Regulates Electron Transferand Superoxide Generation Activities of the Cytochrome bc1 Complex from Rhodobacter sphaeroides
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b00658/20151208/images/medium/bi-2015-006587_0006.gif
Biochemistry
DOI: 10.1021/acs.biochem.5b00658
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The structure and dynamic properties of the complete histidine phosphotransfer domain of the chemotaxis specific histidine autokinase CheA from Thermotoga maritima
The structure and dynamic properties of the complete histidine phosphotransfer domain of the chemotaxis specific histidine autokinase CheA from Thermotoga maritima
Abstract The bacterial histidine autokinase CheA contains a histidine phosphotransfer (Hpt) domain that accepts a phosphate from the catalytic domain and donates the phosphate to either target response regulator protein, CheY or CheB. The Hpt domain forms a helix-bundle structure with a conserved four-helix bundle motif and a variable fifth helix. Observation of two nearly equally populated conformations in the crystal...
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[NMR paper] Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NM
Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NMR.
Biochemistry. 1997 Jan 28;36(4):699-710
Authors: Zhou H, Dahlquist FW
Bacterial chemotaxis involves autophosphorylation of a histidine kinase and transfer of the phosphoryl group to response regulators to control flagellar rotation and receptor adaptation. The...
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08-22-2010 03:31 PM
[NMR paper] Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NM
Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NMR.
Biochemistry. 1997 Jan 28;36(4):699-710
Authors: Zhou H, Dahlquist FW
Bacterial chemotaxis involves autophosphorylation of a histidine kinase and transfer of the phosphoryl group to response regulators to control flagellar rotation and receptor adaptation. The...
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08-22-2010 03:03 PM
[NMR paper] NMR studies of the phosphotransfer domain of the histidine kinase CheA from Escherich
NMR studies of the phosphotransfer domain of the histidine kinase CheA from Escherichia coli: assignments, secondary structure, general fold, and backbone dynamics.
Related Articles NMR studies of the phosphotransfer domain of the histidine kinase CheA from Escherichia coli: assignments, secondary structure, general fold, and backbone dynamics.
Biochemistry. 1995 Oct 24;34(42):13858-70
Authors: Zhou H, Lowry DF, Swanson RV, Simon MI, Dahlquist FW
Multidimensional heteronuclear NMR techniques were applied to study the phosphotransfer domain,...
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[NMR paper] Solution structure of GAP SH3 domain by 1H NMR and spatial arrangement of essential R
Solution structure of GAP SH3 domain by 1H NMR and spatial arrangement of essential Ras signaling-involved sequence.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Solution structure of GAP SH3 domain by 1H NMR and spatial arrangement of essential Ras signaling-involved sequence.
EMBO J. 1994 Mar 15;13(6):1270-9
Authors: Yang YS, Garbay C, Duchesne M, Cornille F, Jullian N, Fromage N, Tocque B, Roques BP
Src homology 3 (SH3) domains are found in numerous...
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[NMR paper] Solution structure of GAP SH3 domain by 1H NMR and spatial arrangement of essential R
Solution structure of GAP SH3 domain by 1H NMR and spatial arrangement of essential Ras signaling-involved sequence.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Solution structure of GAP SH3 domain by 1H NMR and spatial arrangement of essential Ras signaling-involved sequence.
EMBO J. 1994 Mar 15;13(6):1270-9
Authors: Yang YS, Garbay C, Duchesne M, Cornille F, Jullian N, Fromage N, Tocque B, Roques BP
Src homology 3 (SH3) domains are found in numerous...
Dynamic domain arrangement of CheA-CheY complex regulates bacterial thermotaxis, as revealed by NMR.
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