Protein–protein interactions in carotenoid triggered quenching of phycobilisome fluorescence in Synechocystis sp. PCC 6803

AbstractAn inquiry into the effect of temperature on carotenoid triggered quenching of phycobilisome (PBS) fluorescence in a photosystem II-deficient mutant of Synechocystis sp. results in identification of two temperature-dependent processes: one is responsible for the quenching rate, and one determines the yield of PBS fluorescence. Non-Arrhenius behavior of the light-on quenching rate suggests that carotenoid-absorbed light triggers a process that bears a strong resemblance to soluble protein folding, showing temperature-dependent enthalpy of activated complex formation. The response of PBS fluorescence yield to hydration changing additives and to passing of the membrane lipid phase transition point indicates that the pool size of PBSs subject to quenching depends on the state of some membrane component

A putative cytochrome c biogenesis gene in Synechocystis sp. PCC 6803 1The nucleotide sequence of orf334 from Synechocystis sp. PCC 6803 appeared in EMBL and GenBank under accession No. Z72480.1

AbstractA gene (orf334) with homology to chloroplast ycf5 (ccsA) was isolated from the cyanobacterium Synechocystis PCC 6803. The mRNA level of orf334 decreases in the dark and increases rapidly upon illumination. Transcription is initiated 69 nucleotides upstream of the start site of translation. The deduced amino acid sequence of orf334 has limited identity with bacterial proteins involved in cytochrome c biogenesis. Sequence comparison indicates differing pathways of cytochrome c biogenesis in cyanobacteria/chloroplasts and Gram− positive bacteria versus proteobacteria and mitochondria. Insertional inactivation of the orf334 gene gave rise to a heterozygous mutant, i.e. complete absence of the orf334 product seems to be lethal to the cell

State of the phycobilisome determines effective absorption cross-section of Photosystem II in Synechocystis sp. PCC 6803

Quenching of excess excitation energy is necessary for the photoprotection of light-harvesting complexes. In cyanobacteria, quenching of phycobilisome (PBS) excitation energy is induced by the Orange Carotenoid Protein (OCP), which becomes photoactivated under high light conditions. A decrease in energy transfer efficiency from the PBSs to the reaction centers decreases photosystem II (PS II) activity. However, quantitative analysis of OCPinduced photoprotection in vivo is complicated by similar effects of both photochemical and non-photochemical quenching on the quantum yield of the PBS fluorescence overlapping with the emission of chlorophyll. In the present study, we have analyzed chlorophyll a fluorescence induction to estimate the effective cross-section of PS II and compared the effects of reversible OCP-dependent quenching of PBS fluorescence with reduction of PBS content upon nitrogen starvation or mutations of key PBS components. This approach allowed us to estimate the dependency of the rate constant of PS II primary electron acceptor reduction on the amount of PBSs in the cell. We found that OCP-dependent quenching triggered by blue light affects approximately half of PBSs coupled to PS II, indicating that under normal conditions, the concentration of OCP is not sufficient for quenching of all PBSs coupled to PS II