Chloroplastic ATP Synthase Alleviates Photoinhibition of Photosystem I in Tobacco Illuminated at Chilling Temperature.

Chloroplastic ATP synthase plays a significant role in the regulation of proton motive force (pmf) and proton gradient (Delta pH) across the thylakoid membranes. However, the regulation of chloroplastic ATP synthase at chilling temperature and its role in photoprotection are little known. In our present study, we examined the chlorophyll fluorescence, P700 signal, and electrochromic shift signal at 25 degrees C, and 6 degrees C in tobacco (Nicotiana tabacum L.cv. Samsun). Although photosynthetic electron flow through both PSI and PSII were severely inhibited at 6 degrees C, non-photochemical quenching and P700 oxidation ratio were largely increased. During the photosynthetic induction under high light, the formation of pmf at 6 degrees C was similar to that at 25 degrees C. However, the pH was significantly higher at 6 degrees C, owing to the decreased activity of chloroplastic ATP synthase (g(H)(+)). During illumination at 6 degrees C and high light, a high Delta pH made PSI to be highly oxidized, preventing PSI from photoinhibition. These results indicate that the downregulation of g(H)(+) is critical to the buildup of Delta pH at low temperature, adjusting the redox state of PSI, and thus preventing photodamage to PSI. Our findings highlight the importance of chloroplastic ATP synthase in photoprotection at chilling temperature.