Plant Physiology Preview
Published on September 7, 2007; 10.1104/pp.107.105866
OPEN ACCESS ARTICLE
Received July 22, 2007
Accepted September 4, 2007
Distinct Functions for the Two PsbP-Like Proteins PPL1 and PPL2 in the Chloroplast thylakoid Lumen of Arabidopsis
Seiko Ishihara , Atsushi Takabayashi , Kunio Ido , Tsuyoshi Endo , Kentaro Ifuku *, and Fumihiko Sato
Graduate School of Biostudies, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan
* Corresponding author; email: ifuku{at}kais.kyoto-u.ac.jp.
PsbP, an extrinsic subunit of photosystem II (PSII), is a nuclear-encoded protein that optimizes the water-splitting reaction in vivo. In addition to PsbP, higher plants have two nuclear-encoded genes for PsbP homologs (PsbP-like proteins: PPLs) that show significant sequence similarity to a cyanobacterial PsbP homolog (cyanoP); however, the function of PPLs in higher plants has not yet been elucidated. In this study, we characterized Arabidopsis mutants lacking either of two PPLs, PPL1 and PPL2. Phylogenetic analysis suggests that PPL1 would be an ortholog of cyanoP, and PPL2 and PsbP may have paralogous relationship with PPL1. Analysis on mRNA expression profiles showed that PPL1 expressed under stress conditions and PPL2 co-expressed with the subunits of chloroplast NAD(P)H dehydrogenase (NDH) complex. Consistent with these suggestions, photosystem II activity in a ppl1 mutant was more sensitive to high-intensity light than wild-type, and the recovery of photo-inhibited PSII activity was delayed in ppl1 plants. Therefore, PPL1 is required for efficient repair of photodamaged PSII. Furthermore, the stoichometric level and activity of chloroplast NDH complex in thylakoids were severely decreased in a ppl2 mutant, demonstrating that PPL2 is a novel thylakoid lumenal factor required for accumulation of the chloroplast NDH complex. These results suggest that during endosymbiosis and subsequent gene transfer to the host nucleus, cyanoP from ancient cyanobacteria evolved into PPL1, PPL2, and PsbP, and each of them has a distinct role in the photosynthetic electron transfer in Arabidopsis.
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