Temperature-Sensitive Reaction of a Photosensor Protein YcgF: Possibility of a Role of Temperature Sensor
Yusuke Nakasone
Taka-aki Ono
Asako Ishii
Shinji Masuda
Masahide Terazima
10.1021/bi902121z.s001
https://acs.figshare.com/articles/journal_contribution/Temperature_Sensitive_Reaction_of_a_Photosensor_Protein_YcgF_Possibility_of_a_Role_of_Temperature_Sensor/2784088
The 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 BLUFâlinker 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.
2010-03-16 00:00:00
conformation change
Temperature SensorThe
photoinduced reactions
temperature dependence
temperature sensitivity
dimer form
photoreactive species
grating method
light sensor
nonreactive species
Photosensor Protein YcgF
EAL domain
temperature sensor
BLUF
photoreaction
nonreactive YcgF species
light sensor protein YcgF
photoinduced dimerization