Abstract
We have examined the level of photosystem II (PSII) dimers in Synechocystis sp. PCC 6803 strains lacking the individual extrinsic proteins PsbO, PsbU and PsbV. We have also compared the rate of recovery from photodamage in each of these mutants. Removal of PsbO resulted in a mutant with only monomeric PSII while the removal of PsbU created a strain with a similar ratio of dimers to monomers as detected in wild type. In the case of the ▵PsbV mutant a reduced amount of dimers was observed. All three mutants were rapidly photodamaged by high light and recovered to their initial PSII activity under low light. The rate of recovery of the ▵PsbU strain was rapid while that of ▵PsbV cells was slower. The ▵PsbO mutant exhibited an intermediate rate of recovery.
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References
Burnap RL, Qian M, Pierce C (1996) The manganese-stabilizing protein (MSP) of photosystem II modifies the in vivo deactivation and photoactivation kinetics of the H2O-oxidation complex in Synechocystis sp. PCC 6803. Biochemistry 35:874-882.
Clarke SM, Eaton-Rye JJ (1999) Mutation of Phe-363 in the photosystem II protein CP47 impairs photoautotrophic growth, alters the chloride requirement, and prevents photosynthesis in the absence of either PSII-O or PSII-V in Synechocystis sp. PCC 6803. Biochemistry 38:2707-2715.
De Las Rivas J, Barber J (2004) Analysis of the structure of the PsbO protein and its implications. Photosynth Res 81:329-343.
Ferreira KN, Iverson TM, Maghlaoui K, Barber J, Iwata S (2004) Architecture of the photosynthetic oxygen-evolving center. Science 303:1831-1838.
Inoue-Kashino N, Kashino Y, Satoh K, Terashima I, Pakrasi HB (2005) PsbU provides a stable architecture for the oxygen-evolving system in cyanobacterial photosystem II . Biochemistry 44:12214-12228.
Loll B, Kern J, Saenger W, Zouni A, Biesiadka J (2005) Towards complete cofactor arrangement in the 3.0 Å resolution structure of photosystem II. Nature 438:1040-1044.
Morgan TR, Shand JA, Clarke SM, Eaton-Rye JJ (1998) Specific requirements for cytochrome c-550 and the manganese-stabilizing protein in photoautotrophic strains of Synechocystis sp. PCC 6803 with mutations in the domain Gly-351to Thr-436 of the chlorophyll-binding protein CP47. Biochemistry 37:14437-14449.
Nowaczyk MM, Hebeler R, Schlodder E, Meyer HE, Warscheid B, Rögner M (2006) Psb27, a cyanobacterial lipoprotein, is involved in the repair cycle of photosystem II. Plant Cell 18:3121-3131.
Rokka A, Suorsa M, Saleem A, Battchikova N, Aro E-M (2005) Synthesis and assembly of thylakoid protein complexes: Multiple assembly steps of photosystem II. Biochem J 388:159-168.
Roose JL, Wegener KM, Pakrasi HB (2007) The extrinsic proteins of photosystem II. Photosynth Res 92:369-387.
Shen JR, Vermaas W, Inoue Y (1995) The role of cytochrome c550 as studied through reverse genetics and mutant characterization in Synechocystis sp. PCC 6803. J Biol Chem 270:6901-6907.
Summerfield TC, Shand JA, Bentley FK, Eaton-Rye JJ (2005) PsbQ (Sll1638) in Synechocystis sp. PCC 6803 is required for photosystem II activity in specific mutants and in nutrient-limiting conditions. Biochemistry 44:805-815.
Veerman J, Bentley FK, Eaton-Rye JJ, Mullineaux CW, Vasil’ev S, Bruce D (2005) The PsbU subunit of photosystem II stabilizes energy transfer and primary photochemistry in the phycobilisome-photosystem II assembly of Synechocystis sp. PCC 6803. Biochemistry 44:16939-16948.
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Bentley, F.K., Eaton-Rye, J.J. (2008). The Effect of Removing Photosystem II Extrinsic Proteins on Dimer Formation and Recovery from Photodamage in Synechocystis sp. PCC 6803. In: Allen, J.F., Gantt, E., Golbeck, J.H., Osmond, B. (eds) Photosynthesis. Energy from the Sun. Springer, Dordrecht. https://doi.org/10.1007/978-1-4020-6709-9_159
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DOI: https://doi.org/10.1007/978-1-4020-6709-9_159
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