Journal
JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY
Volume 224, Issue -, Pages -Publisher
ELSEVIER SCIENCE SA
DOI: 10.1016/j.jphotobiol.2021.112305
Keywords
Chloroplast movement; Gene duplication; Liverwort; LOV domain; Photocycle; Phototropin
Categories
Funding
- Japan Society for the Promotion of Science KAKENHI [18H02455]
- MEXT KAKENHI [JP20H05910]
- Japan Science and Technology Agency, Exploratory Research for Advanced Technology, Numata Organelle Reaction Cluster [JPMJER1602]
- Grants-in-Aid for Scientific Research [18H02455] Funding Source: KAKEN
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This study investigates the functional differences of the photoreceptor Phototropin (phot) in plants, specifically focusing on the light-oxygen-voltage (LOV) domains in species with duplication events and those without. The research reveals that even in unduplicated liverworts, Mpphot exhibits some similar functions to duplicated photosensitive proteins, highlighting conservation and diversification among LOV domains in the evolution of land plants.
Phototropin (phot) is a blue light photoreceptor in plants and possesses two photosensory light-oxygen-voltage (LOV1 and LOV2) domains with different photo-thermochemical properties. While liverworts contain a single copy of PHOT (e.g., MpPHOT in Marchantia polymorpha), many land plant species contain multicopy PHOT genes (e.g., AtPHOT1 and 2 in Arabidopsis thaliana) due to evolutionary gene duplication. The LOV domains of duplicated phot proteins have been studied in detail, but those of single-copy phot proteins remain to be characterized. As phot has not been duplicated in liverworts, we hypothesized that Mpphot may retain the ancestral function and photo-thermochemical properties. To learn more about the unduplicated phot proteins, we analyzed chloroplast relocation movement and the photo-thermochemical properties of LOV1 and LOV2 in Mpphot (Mpphot-LOV1 and Mpphot-LOV2, respectively). The function of Mpphot-LOV1, which induced a response to move chloroplasts to weak light (the accumulation response) in the absence of photoactive LOV2, differed from that of LOV1 of the duplicated phot proteins of A. thaliana (e.g., Atphot1-LOV1 preventing the accumulation response). On the other hand, the function of Mpphot-LOV2 was similar to that of LOV2 of the duplicated phots. The photo-thermochemical properties of Mpphot were a hybrid of those of the duplicated phots; the photochemical and thermochemical reactions of Mpphot were similar to those of the phot2- and phot1-type proteins, respectively. Our findings reveal conservation and diversification among LOV domains during phot duplication events in land plant evolution.
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