Dynamic domain arrangement of CheA-CheY complex regulates bacterial thermotaxis, as revealed by NMR
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 dyna...
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| Veröffentlicht in: | Scientific reports 2017-11, Vol.7 (1), p.16462-17, Article 16462 |
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| description | 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. |
| doi_str_mv | 10.1038/s41598-017-16755-x |
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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. 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| subjects | 101/6 631/45/612/1234 631/535/878/1263 631/553/2710 Attractants CheA protein CheY protein Humanities and Social Sciences multidisciplinary NMR Nuclear magnetic resonance Repellents Science Science (multidisciplinary) Signal transduction Temperature effects Thermotaxis |
| title | Dynamic domain arrangement of CheA-CheY complex regulates bacterial thermotaxis, as revealed by NMR |
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