Fig. 1: Overall architecture and UV-vis spectroscopy of DrBphP, Agp1, and their Chimera with and without their cognate response regulator. | Nature Communications

Fig. 1: Overall architecture and UV-vis spectroscopy of DrBphP, Agp1, and their Chimera with and without their cognate response regulator.

From: Comparative analysis of two paradigm bacteriophytochromes reveals opposite functionalities in two-component signaling

Fig. 1

a Schematic representation of a canonical bacteriophytochrome with a histidine kinase (HK) effector domain. The site of the phosphorylated histidine is indicated as the letter P. In addition, a schematic presentation of the phytochrome chimera is shown, where the photosensory module (PSM) of DrBphP is combined with the HK domain of Agp1. Abbreviations: Period/ARNT/single-minded (PAS), cGMP phosphodiesterase/adenylyl cyclase/FhlA (GAF), phytochrome-specific (PHY), histidine kinase (HK), dimerization Histidine phosphotransfer domain (DHp), catalytic ATP-binding domain (CA). b The absorption spectra of the BphP HKs with and without their cognate response regulators (RR) in dark (D) or under red light (R). The right-most panels show their dark reversion kinetics as an A750/A700 ratio over time, where 0 min corresponds to the time the 655-nm illumination ceased. Source data are provided as a Source data file.

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