Cyclic electron flow (CEF) around photosystem I has a role in avoiding photoinhibition of photosystem II (PSII), which occurs under conditions in which the rate of photodamage to PSII exceeds the rate of its repair. However, the molecular mechanism underlying how CEF contributes to photoprotection is not yet well understood. We examined the effect of impairment of CEF and thermal energy dissipation (qE) on photoinhibition using CEF (pgr5) and qE (npq1 and npq4) mutants of Arabidopsis (Arabidopsis thaliana) exposed to strong light. Impairment of CEF by mutation of pgr5 suppressed qE and accelerated photoinhibition. We found that impairment of qE, by mutations of pgr5, npq1, and npq4, caused inhibition of the repair of photodamaged PSII at the step of the de novo synthesis of the D1 protein. In the presence of the chloroplast protein synthesis inhibitor chloramphenicol, impairment of CEF, but not impairment of qE, accelerated photoinhibition, and a similar effect was obtained when leaves were infiltrated with the protonophore nigericin. These results suggest that CEF-dependent generation of DpH across the thylakoid membrane helps to alleviate photoinhibition by at least two different photoprotection mechanisms: one is linked to qE generation and prevents the inhibition of the repair of photodamaged PSII at the step of protein synthesis, and the other is independent of qE and suppresses photodamage to PSII.

The production of oxygen and the supply of energy for life on earth rely on the process of photosynthesis using sunlight. Paradoxically, sunlight damages the photosynthetic machinery, primarily photosystem II (PSII), leading to photoinhibition and loss of plant performance. However, there is uncertainty about which wavelengths are most damaging to PSII under sunlight. In this work we examined this in a simple experiment where Arabidopsis (Arabidopsis thaliana) leaves were exposed to different wavelengths of sunlight by dispersing the solar radiation across the surface of the leaf via a prism. To isolate only the process of photodamage, the repair of photodamaged PSII was inhibited by infiltration of chloramphenicol into the exposed leaves. The extent of photodamage was then measured as the decrease in the maximum quantum yield of PSII using an imaging pulse amplitude modulation fluorometer. Under the experimental light conditions, photodamage to PSII occurred most strongly in regions exposed to ultraviolet (UV) or yellow light. The extent of UV photodamage under incident sunlight would be greater than we observed when one corrects for the optical efficiency of our system. Our results suggest that photodamage to PSII under sunlight is primarily associated with UV rather than photosynthetically active light wavelengths.Plants absorb sunlight to power the productive photochemical reactions of photosynthesis. Absorption of sunlight may also lead to deleterious photochemistry that damages the photosynthetic machinery. The PSII protein complex is important in this regard as it seems to be most susceptible to photodamage that results in photoinhibition and ultimately suppresses photosynthetic CO 2 assimilation, growth, and productivity (Long et al., 1994;Takahashi and Murata, 2008). Although plants have photoprotection mechanisms (Niyogi, 1999) and can effectively repair photodamaged PSII through the PSII repair cycle (Aro et al., 1993), photoinhibition still occurs under stressful environmental conditions Murata et al., 2007;Takahashi and Murata, 2008).The onset of photoinhibition is strongly correlated with the absorption of excessive excitation energy for photosynthesis. Therefore, photodamage to PSII was most readily assumed to be attributed to the excess light absorbed by photosynthetic pigments (Melis, 1999). However, the extent of photodamage that is measured under conditions where the repair of photodamaged PSII is prevented by inhibiting chloroplast protein synthesis (i.e. lincomycin or chloramphenicol) is directly proportional to the intensity of light (Mattoo et al., 1984; Tyystjärvi and Aro, 1996;Nishiyama et al., 2001Nishiyama et al., , 2004Allakhverdiev and Murata, 2004;Chow et al., 2005). Furthermore, recent studies have demonstrated that interruption of the Calvin cycle (Hakala et al., 2005;Takahashi and Murata, 2005;Takahashi et al., 2007) and inhibition of electron transfer between Q A and Q B (Jegerschö ld et al., 1990;Kirilovsky et al., 1994;Allakhverdiev et al., 2005) have no effect on the rate of ...

Bundle Sheath Defective 2, BSD2, is a stroma-targeted protein initially identified as a factor required for the biogenesis of ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO) in maize. Plants and algae universally have a homologous gene for BSD2 and its deficiency causes a RuBisCO-less phenotype. As RuBisCO can be the rate-limiting step in CO 2 assimilation, the overexpression of BSD2 might improve photosynthesis and productivity through the accumulation of RuBisCO. To examine this hypothesis, we produced BSD2 overexpression lines in Arabidopsis. Compared with wild type, the BSD2 overexpression lines BSD2ox-2 and BSD2ox-3 expressed 4.8-fold and 8.8-fold higher BSD2 mRNA, respectively, whereas the empty-vector (EV) harbouring plants had a comparable expression level. The overexpression lines showed a significantly higher CO 2 assimilation rate per available CO 2 and productivity than EV plants. The maximum carboxylation rate per total catalytic site was accelerated in the overexpression lines, while the number of total catalytic sites and RuBisCO content were unaffected. We then isolated recombinant BSD2 (rBSD2) from E. coli and found that rBSD2 reduces disulfide bonds using reductants present in vivo, for example glutathione, and that rBSD2 has the ability to reactivate RuBisCO that has been inactivated by oxidants. Furthermore, 15% of RuBisCO freshly isolated from leaves of EV was oxidatively inactivated, as compared with 0% in BSD2-overexpression lines, suggesting that the overexpression of BSD2 maintains RuBisCO to be in the reduced active form in vivo. Our results demonstrated that the overexpression of BSD2 improves photosynthetic efficiency in Arabidopsis and we conclude that it is involved in mediating RuBisCO activation.