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PSB27: A thylakoid protein enabling Arabidopsis to adapt to changing light intensity

Our results provide evidence that PSB27, a soluble protein of the chloroplast thylakoid lumen, is essential for enabling plants to adapt to changes in light intensity. Adaptation takes place independently of photosystem II supercomplexes and, based on work of others, of state transitions for the redistribution of light harvesting proteins. This finding opens the door to pursue the question of how photosynthesis adjusts to fluctuating sunlight and enables plants to grow under ever-changing environmental conditions.

Xin Hou, Aigen Fu, Veder J. Garcia, Bob B. Buchanan, and Sheng Luan

 

Significance

 

Our results provide evidence that PSB27, a soluble protein of the chloroplast thylakoid lumen, is essential for enabling plants to adapt to changes in light intensity. Adaptation takes place independently of photosystem II supercomplexes and, based on work of others, of state transitions for the redistribution of light harvesting proteins. This finding opens the door to pursue the question of how photosynthesis adjusts to fluctuating sunlight and enables plants to grow under ever-changing environmental conditions.

 

Abstract

 

In earlier studies we have identified FKBP20-2 and CYP38 as soluble proteins of the chloroplast thylakoid lumen that are required for the formation of photosystem II supercomplexes (PSII SCs). Subsequent work has identified another potential candidate functional in SC formation (PSB27). We have followed up on this possibility and isolated mutants defective in the PSB27 gene. In addition to lack of PSII SCs, mutant plants were severely stunted when cultivated with light of variable intensity. The stunted growth was associated with lower PSII efficiency and defective starch accumulation. In response to high light exposure, the mutant plants also displayed enhanced ROS production, leading to decreased biosynthesis of anthocyanin. Unexpectedly, we detected a second defect in the mutant, namely in CP26, an antenna protein known to be required for the formation of PSII SCs that has been linked to state transitions. Lack of PSII SCs was found to be independent of PSB27, but was due to a mutation in the previously described cp26 gene that we found had no effect on light adaptation. The present results suggest that PSII SCs, despite being required for state transitions, are not associated with acclimation to changing light intensity. Our results are consistent with the conclusion that PSB27 plays an essential role in enabling plants to adapt to fluctuating light intensity through a mechanism distinct from photosystem II supercomplexes and state transitions.

 

See: http://www.pnas.org/content/112/5/1613.abstract.html?etoc

PNAS February 3, 2015; vol.112, no.5: 1613–1618

 

Fig. 5. Genetic linkage of cp26 and psb27 mutant alleles with plant growth defects. (A) The original T-DNA ML containing both cp26 and psb27 mutant alleles was compared with the WT and with segregated single mutants of cp26 and psb27 under constant light intensity in a growth chamber (Upper) or under varying light intensity in a greenhouse (Lower). (B) The plants were grown on 1/2 MS medium in growth chamber (Left) or greenhouse (Center) for 10 d. The same plants grown under constant low light for 10 d were then transferred to high light (350 μmol m−2 s−1) for 2 d (Right). (C) Blue native gel analysis showing PSII SCs of thylakoid proteins of WT, ML, psb27, cp26, ML complemented with CP26 or/and PSB27. (D) Tris-Tricine SDS PAGE analyses showing CP26 proteins of thylakoids of the same plants in C.

 

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