The nuclear-encoded chlorophyll-binding photosystem II-S protein is stable in the absence of pigments.

The 22-kDa chlorophyll a/b-binding protein (CAB) (psbS gene product) is associated with photosystem II and related to the CAB gene family. Here we report that the PSII-S protein unlike other chlorophyll-binding proteins is stable in the absence of pigments. It is present in etiolated spinach plants and accumulates in the dark progressively with the cellular development of the seedlings. Furthermore, it is present in several pigment-deficient mutants. Analysis of the pigment composition of the PSII-S protein isolated from etiolated plants suggests that neither carotenoids nor chlorophyll precursors are involved in its stabilization in the dark. Exposure of etiolated spinach to light leads to further accumulation of the PSII-S protein, which appears more early than other chlorophyll-binding proteins. Accumulation of the PSII-S protein in green plants is developmentally regulated and restricted to photosynthetic tissues. It is suggested that the function of the PSII-S protein may not be light-harvesting but it could act as a ligand chaperone required for transient binding of pigments during biogenesis or turnover of chlorophyll-binding proteins. Such function would be essential for coordination between pigment biosynthesis and ligation as well as avoiding toxic effects of non-bound chlorophyll molecules.