However, PMM1416 has been seen to be upregulated during both P an

However, PMM1416 has been seen to be upregulated during both P and light stress, indicating a general stress response role for this particular protein (Coleman et al., 2006). The levels of alkaline phosphatase, PhoA, were c. 28-fold more abundant in the stressed cultures, whereas the porin PhoE was c. 50-fold more abundant (Fig. 2a). At the transcriptomic level after 48 h, the regulated levels were almost at parity (Martiny et al., 2006), suggesting the differential production of both PhoE and PhoA over extended starvation periods. Increased alkaline phosphatase activity has been measured previously for oceanic picocyanobacteria under P stress

(Moore et al., 2005; Tetu et al., 2009) and in Synechocystis sp. PCC6803 (Gan, 2006), NVP-BKM120 manufacturer and so our results are in line with these observations. The structure and functioning of the MED4 photosynthetic apparatus is affected through extended P starvation (Fig. 3). Seven proteins were recognized as differentially abundant (Fig. 2b). Proteins that were less abundant than the control were those associated with chlorophyll binding and light harvesting (e.g. Pcb and CP43 within PSII). Interestingly, this observation has also been identified

recently at the transcriptomic level in Synechococcus WH8102 when subjected to extended P stress (Tetu et al., 2009). PsaA, which is known to be an electron acceptor in PSI, is also less abundant as well as the plastocyanin docking protein PsaF. PsaA is also a vital part of the photosynthetic

electron transport chain (PETC), and binds almost 100 chlorophyll molecules, making it an essential light-harvesting protein Methamphetamine in PSI (Barber, 2001), specifically as MED4 has only one copy of the pcb gene, which is associated exclusively with PSII (Fig. 3) (Rocap et al., 2003). From this, we conclude that the cell reduced its photosynthetic capabilities. This would directly reduce UV photodamage and oxidative stress from reactive oxygen species produced as a byproduct of water splitting at the oxygen-evolving complex at the base of PSII. This conclusion is supported by the observation that the known antioxidants, thioredoxin (TrxA) and thioredoxin peroxidise (tpx), are not significantly differentially abundant in the stressed phenotype (Fig. 2d). It is also clear that other essential proteins in the PETC, besides PsaF, are less abundant than the P-replete control. PsaF and ferredoxin-NADP oxidoreductase are downregulated, which strongly suggests that the cell is attempting to reduce certain reductive energy production processes, specifically NADPH generation, which in turn indicates a general metabolic slowdown. It is interesting to note that essential protein subunits of the ATP synthase complex are unaffected by long-term exposure to P deprivation, which suggests that ATP was produced normally.

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