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Temperature-Sensitive Reaction of a Photosensor Protein YcgF: Possibility of a Role of Temperature Sensor
journal contribution
posted on 2010-03-16, 00:00 authored by Yusuke Nakasone, Taka-aki Ono, Asako Ishii, Shinji Masuda, Masahide TerazimaThe spectrally silent photoreaction of a blue light sensor protein YcgF, composed of the N-terminal BLUF domain and the C-terminal EAL domain, was investigated by the time-resolved transient grating method. Comparing photoinduced reactions of full-length YcgF with that of the BLUF−linker construct, it was found that a major conformation change after photoinduced dimerization is predominantly localized on the EAL domain. Furthermore, the photoinduced conformational change displayed significant temperature dependence. This result is explained by an equilibrium of reactive and nonreactive YcgF species, with the population of photoreactive species decreasing as the temperature is lowered in the dark state. We consider that the dimer form is the nonreactive species and it is the dominant species at lower temperatures. The temperature sensitivity of the photoreaction of YcgF suggests that this protein could have a biological function as a temperature sensor as well as behaving as a light sensor.
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conformation changeTemperature SensorThephotoinduced reactionstemperature dependencetemperature sensitivitydimer formphotoreactive speciesgrating methodlight sensornonreactive speciesPhotosensor Protein YcgFEAL domaintemperature sensorBLUFphotoreactionnonreactive YcgF specieslight sensor protein YcgFphotoinduced dimerization
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