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A significant fraction of a plant's nuclear genome encodes chloroplast-targeted proteins, many of which are devoted to the assembly and function of the photosynthetic apparatus. Using digital video imaging of chlorophyll fluorescence, we isolated  proton gradient regulation 7  ( pgr7 ) as an  Arabidopsis thaliana  mutant with low nonphotochemical quenching of chlorophyll fluorescence (NPQ). In  pgr7 , the xanthophyll cycle and the  PSBS  gene product, previously identified NPQ factors, were still functional, but the efficiency of photosynthetic electron transport was lower than in the wild type. The  pgr7  mutant was also smaller in size and had lower chlorophyll content than the wild type in optimal growth conditions. Positional cloning located the  pgr7  mutation in the  At3g21200  ( PGR7 ) gene, which was predicted to encode a chloroplast protein of unknown function. Chloroplast targeting of PGR7 was confirmed by transient expression of a GFP fusion protein and by stable expression and subcellular localization of an epitope-tagged version of PGR7. Bioinformatic analyses revealed that the PGR7 protein has two domains that are conserved in plants, algae, and bacteria, and the N-terminal domain is predicted to bind a cofactor such as FMN. Thus, we identified  PGR7  as a novel, conserved nuclear gene that is necessary for efficient photosynthetic electron transport in chloroplasts of Arabidopsis.

Arabidopsis thaliana PGR7 Encodes a Conserved Chloroplast Protein That Is Necessary for Efficient Photosynthetic Electron Transport