ArticleScientific reports2017
Dynamic domain arrangement of CheA-CheY complex regulates bacterial thermotaxis, as revealed by NMR.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Genome analysis of a halophilicFrontiers in microbiology · 2023Article
- Role of Position K+4 in the Phosphorylation and Dephosphorylation Reaction Kinetics of the CheY Response Regulator.Biochemistry · 2021Article
- Structural equilibrium underlying ligand-dependent activation of βNature chemical biology · 2020Article
- NMR Structure and Dynamics of TonB Investigated by Scar-Less Segmental Isotopic Labeling Using a Salt-Inducible Split Intein.Frontiers in chemistry · 2020Article
- Segmental isotopic labeling by asparaginyl endopeptidase-mediated protein ligation.Journal of biomolecular NMR · 2018Article
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Authors and funding
5 authors.
Funding
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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.
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