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The capacity for photosynthetic acclimation in Arabidopsis thaliana (L.) Heynh. cv. Landsberg erecta was assessed during growth over a broad range of irradiance. Discontinuities in the response to growth irradiance were revealed for the light- and CO2-saturated rate of photosynthesis (Pmax) and the ratio of chlorophyll a to chlorophyll b (Chl a/b). Three separate phases in the response of Pmax and Chl a/b to growth light were evident, with increases at low and high irradiance ranges and a plateau at intermediate irradiance. By measuring all chlorophyll-containing components of the thylakoid membrane that contribute to Chl a/b we reveal that distinct strategies for growth at low and high irradiance underlie the discontinuous response. These strategies include, in addition to changes in the major light-harvesting complexes of photosystem II (LHCII), large shifts in the amounts of both reaction centres as well as significant changes in the levels of minor LHCII and LHCI components.

Using a var2-2 mutant of Arabidopsis thaliana, which lacks a homologue of the zinc-metalloprotease, FtsH, we demonstrate that this protease is required for the efficient turnover of the D1 polypeptide of photosystem II and protection against photoinhibition in vivo. We show that var2-2 leaves are much more susceptible to lightinduced photosystem II photoinhibition than wild-type leaves. Furthermore, the rate of photosystem II photoinhibition in untreated var2-2 leaves is equivalent to that of var2-2 and wild-type leaves, which have been treated with lincomycin, an inhibitor of the photosystem II repair cycle at the level of D1 synthesis. This is in contrast to untreated wild-type leaves, which show a much slower rate of photosystem II photoinhibition due to an efficient photosystem II repair cycle. The recovery of var2-2 leaves from photosystem II photoinhibition is also impaired relative to wild-type. Using Western blot analysis in the presence of lincomycin we show that the D1 polypeptide remains stable in leaves of the var2-2 mutant under photoinhibitory conditions that lead to D1 degradation in wild-type leaves and that the abundance of DegP2 is not affected by the var2-2 mutation. We conclude, therefore, that the Var2 FtsH homologue is required for the cleavage of the D1 polypeptide in vivo. In addition, we identify a conserved lumenal domain in Var2 that is unique to FtsH homologues from oxygenic phototrophs. The Photosystem II (PSII)1 complex is a large protein-pigment assembly that catalyzes the light-dependent oxidation of water to molecular oxygen in chloroplasts and cyanobacteria. At the core of PSII lies the D1/D2 heterodimer, which binds the pigments and co-factors necessary for primary photochemistry (1). The D1 polypeptide is also important because of its high rate of turnover (2). This high turnover rate is related to the vulnerability of PSII to light, with D1 being the main target for photoinactivation and subsequent damage. An efficient repair cycle for D1 is therefore of paramount importance in oxygenic phototrophs. When the rate of photoinactivation and damage of D1 exceeds the capacity for repair, photoinhibition occurs, resulting in a decrease in the maximum efficiency of PSII photochemistry.A key feature of the D1 repair cycle is the degradation of the damaged polypeptide. It is generally accepted that damaged D1 is initially cleaved at a site on the stromal loop between transmembrane helices D and E yielding a 23-kDa N-terminal fragment (3) and a 10-kDa C-terminal fragment (4). This cleavage step is believed to be initiated by structural changes within the D1 polypeptide (5), although the precise nature of the cleavage event remains unclear. One proposal is that the action of active oxygen species acts to cleave the D1 polypeptide during strong illumination (6). However, the temperature dependence of the process (7) and its sensitivity to protease inhibitors (8) indicates the involvement of enzymatic proteolysis by an unidentified protease. Following cleavage, the breakdown fragments of ...

When plants, algae, and cyanobacteria are exposed to excessive light, especially in combination with other environmental stress conditions such as extreme temperatures, their photosynthetic performance declines. A major cause of this photoinhibition is the light-induced irreversible photodamage to the photosystem II (PSII) complex responsible for photosynthetic oxygen evolution. A repair cycle operates to selectively replace a damaged D1 subunit within PSII with a newly synthesized copy followed by the light-driven reactivation of the complex. Net loss of PSII activity occurs (photoinhibition) when the rate of damage exceeds the rate of repair. The identities of the chaperones and proteases involved in the replacement of D1 in vivo remain uncertain. Here, we show that one of the four members of the FtsH family of proteases (cyanobase designation slr0228) found in the cyanobacterium Synechocystis sp PCC 6803 is important for the repair of PSII and is vital for preventing chronic photoinhibition. Therefore, the ftsH gene family is not functionally redundant with respect to the repair of PSII in this organism. Our data also indicate that FtsH binds directly to PSII, is involved in the early steps of D1 degradation, and is not restricted to the removal of D1 fragments. These results, together with the recent analysis of ftsH mutants of Arabidopsis, highlight the critical role played by FtsH proteases in the removal of damaged D1 from the membrane and the maintenance of PSII activity in vivo.

Phytoplankton communities in the Ross Sea, Antarctica, are characterized by the haptophyte Phaeocystis antarctica Karsten, which dominates deep mixed layers, and diatoms, including Fragilariopsis cylindrus Grunow, that thrive in shallower mixed layers. To investigate whether differences in photoprotective strategies explain these distributions, photosynthetic parameters, pigments, and fluorescence properties were measured in cultures grown under several irradiance regimes and during acclimation to increased irradiance. In P. antarctica, cellular concentrations of all pigments declined with increasing growth irradiance under continuous light, but xanthophyll cycle pigment concentrations increased with increasing irradiance under dynamic conditions without changes in chlorophyll. In contrast, F. cylindrus exhibited declines in chlorophyll cell 21 with increasing irradiance under both continuous and dynamic conditions, but xanthophyll cycle cell 21 pigments increased under continuous irradiance and declined under dynamic irradiance. P. antarctica did not exhibit non-photochemical quenching (NPQ) unless exposed to irradiance in excess of the mean growth irradiance. F. cylindrus exhibited NPQ in response to lower irradiances but displayed less photoinhibitory quenching than P. antarctica after exposure to very high irradiance. Inhibitor experiments suggest that both taxa rely upon xanthophyll cycle photoprotection to maintain photosynthetic performance but only P. antarctica relies heavily upon protein synthesis, presumably for D1 protein repair. F. cylindrus can thrive in shallow mixed layers because its high capacity for heat dissipation minimizes photoinhibition. P. antarctica utilizes xanthophyll cycle photoprotection to a lesser degree, but is able to dominate deeper mixed layers by effectively repairing the photodamage incurred when it is mixed to the surface.

Cyanobacteria dominate the world's oceans where iron is often barely detectable. One manifestation of low iron adaptation in the oligotrophic marine environment is a decrease in levels of iron-rich photosynthetic components, including the reaction center of photosystem I and the cytochrome b6f complex [R.F. Strzepek and P.J. Harrison, Photosynthetic architecture differs in coastal and oceanic diatoms, Nature 431 (2004) 689-692.]. These thylakoid membrane components have well characterised roles in linear and cyclic photosynthetic electron transport and their low abundance creates potential impediments to photosynthetic function. Here we show that the marine cyanobacterium Synechococcus WH8102 exhibits significant alternative electron flow to O2, a potential adaptation to the low iron environment in oligotrophic oceans. This alternative electron flow appears to extract electrons from the intersystem electron transport chain, prior to photosystem I. Inhibitor studies demonstrate that a propyl gallate-sensitive oxidase mediates this flow of electrons to oxygen, which in turn alleviates excessive photosystem II excitation pressure that can often occur even at relatively low irradiance. These findings are also discussed in the context of satisfying the energetic requirements of the cell when photosystem I abundance is low.

The transcription of S-PM2 phage following infection of Synechococcus sp. WH7803, a marine cyanobacterium, was analysed by quantitative real-time PCR. Unlike the distantly related coliphage T4, there were only two (early and late) instead of three (early, middle and late) classes of transcripts during the developmental cycle of the phage. This difference is consistent with the absence from the S-PM2 genome of T4-like middle mode promoter sequences and the transcription factors associated with their recognition. Phage S-PM2 carries the 'photosynthetic' genes psbA and psbD that encode homologues of the host photosystem II proteins D1 and D2. Transcripts of the phage psbA gene appeared soon after infection and remained at high levels until lysis. Throughout the course of infection, the photosynthetic capacity of the cells remained constant. A considerable transient increase in the abundance of the host psbA transcripts occurred shortly after infection, suggesting that the host responds to the trauma of phage infection in a similar way as it does to a variety of other environmental stresses. The very substantial transcription of the phage psbA gene during the latter phase of phage infection suggests that S-PM2 has acquired this cellular gene to ensure that D1 levels and thus photosynthesis are fully maintained until the infected cell finally lyses. Unexpectedly, transcripts of a phage-encoded S-layer protein gene were among the earliest and most abundant detected, suggesting that this partial homologue of a host protein plays an important role in the S-PM2 infection process.

Adaptation of photosynthesis in marine environment has been examined in two strains of the green, picoeukaryote Ostreococcus: OTH95, a surface/high-light strain, and RCC809, a deep-sea/lowlight strain. Differences between the two strains include changes in the light-harvesting capacity, which is lower in OTH95, and in the photoprotection capacity, which is enhanced in OTH95. Furthermore, RCC809 has a reduced maximum rate of O2 evolution, which is limited by its decreased photosystem I (PSI) level, a possible adaptation to Fe limitation in the open oceans. This decrease is, however, accompanied by a substantial rerouting of the electron flow to establish an H2O-to-H2O cycle, involving PSII and a potential plastid plastoquinol terminal oxidase. This pathway bypasses electron transfer through the cytochrome b6f complex and allows the pumping of ''extra'' protons into the thylakoid lumen. By promoting the generation of a large ⌬pH, it facilitates ATP synthesis and nonphotochemical quenching when RCC809 cells are exposed to excess excitation energy. We propose that the diversion of electrons to oxygen downstream of PSII, but before PSI, reflects a common and compulsory strategy in marine phytoplankton to bypass the constraints imposed by light and/or nutrient limitation and allow successful colonization of the open-ocean marine environment. marine environment ͉ PTOX ͉ water cycle ͉ eletron flow ͉ photoprotection