scholarly journals Protection of the Oxygen-Evolving Machinery by the Extrinsic Proteins of Photosystem II is Essential for Development of Cellular Thermotolerance in Synechocystis sp. PCC 6803

2002 ◽  
Vol 43 (8) ◽  
pp. 932-938 ◽  
Author(s):  
Aiko Kimura ◽  
Julian J. Eaton-Rye ◽  
Eugene H. Morita ◽  
Yoshitaka Nishiyama ◽  
Hidenori Hayashi
Keyword(s):  
Photosystem Ii ◽  
Extrinsic Proteins ◽  
Oxygen Evolving ◽  
Synechocystis Sp ◽  
Pcc 6803

Oxygen-evolving photosystem II preparation from wild-type and photosystem II mutants of Synechocystis sp. PCC 6803

Biochemistry ◽  
1992 ◽  
Vol 31 (7) ◽  
pp. 2099-2107 ◽  
Author(s):  
Diana L. Kirilovsky ◽  
Alain G. P. Boussac ◽  
Frans J. E. Van Mieghem ◽  
Jean Marc R. C. Ducruet ◽  
Pierre R. Setif ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Wild Type ◽  
Oxygen Evolving ◽  
Synechocystis Sp ◽  
Pcc 6803

scholarly journals Cloning of the psbK gene from Synechocystis sp. PCC 6803 and characterization of photosystem II in mutants lacking PSII-K

1991 ◽  
Vol 266 (17) ◽  
pp. 11111-11115
Author(s):  
M. Ikeuchi ◽  
B. Eggers ◽  
G.Z. Shen ◽  
A. Webber ◽  
J.J. Yu ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Synechocystis Sp ◽  
Pcc 6803

scholarly journals Subunit composition of CP43-less photosystem II complexes of Synechocystis sp. PCC 6803: implications for the assembly and repair of photosystem II

2012 ◽  
Vol 367 (1608) ◽  
pp. 3444-3454 ◽  
Author(s):  
M. Boehm ◽  
J. Yu ◽  
V. Reisinger ◽  
M. Beckova ◽  
L. A. Eichacker ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Gel Electrophoresis ◽  
Photochemical Activity ◽  
Subunit Composition ◽  
Null Mutant ◽  
Trap Potential ◽  
Native Gel ◽  
Oxygen Evolving ◽  
Pcc 6803

Photosystem II (PSII) mutants are useful experimental tools to trap potential intermediates involved in the assembly of the oxygen-evolving PSII complex. Here, we focus on the subunit composition of the RC47 assembly complex that accumulates in a psbC null mutant of the cyanobacterium Synechocystis sp. PCC 6803 unable to make the CP43 apopolypeptide. By using native gel electrophoresis, we showed that RC47 is heterogeneous and mainly found as a monomer of 220 kDa. RC47 complexes co-purify with small Cab-like proteins (ScpC and/or ScpD) and with Psb28 and its homologue Psb28-2. Analysis of isolated His-tagged RC47 indicated the presence of D1, D2, the CP47 apopolypeptide, plus nine of the 13 low-molecular-mass (LMM) subunits found in the PSII holoenzyme, including PsbL, PsbM and PsbT, which lie at the interface between the two momomers in the dimeric holoenzyme. Not detected were the LMM subunits (PsbK, PsbZ, Psb30 and PsbJ) located in the vicinity of CP43 in the holoenzyme. The photochemical activity of isolated RC47-His complexes, including the rate of reduction of P680 + , was similar to that of PSII complexes lacking the Mn 4 CaO 5 cluster. The implications of our results for the assembly and repair of PSII in vivo are discussed.

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