Binding and Functional Properties of Four Extrinsic Proteins of Photosystem II from a Red Alga,Cyanidium caldarium, As Studied by Release−Reconstitution Experiments

Biochemistry ◽  
1998 ◽  
Vol 37 (9) ◽  
pp. 2787-2793 ◽  
Author(s):  
Isao Enami ◽  
Sanae Kikuchi ◽  
Tetsuya Fukuda ◽  
Hisataka Ohta ◽  
Jian-Ren Shen
Keyword(s):  
Photosystem Ii ◽  
Functional Properties ◽  
Red Alga ◽  
Cyanidium Caldarium ◽  
Extrinsic Proteins

scholarly journals Binding and Functional Properties of Five Extrinsic Proteins in Oxygen-evolving Photosystem II from a Marine Centric Diatom,Chaetoceros gracilis

2010 ◽  
Vol 285 (38) ◽  
pp. 29191-29199 ◽  
Author(s):  
Ryo Nagao ◽  
Akira Moriguchi ◽  
Tatsuya Tomo ◽  
Ayako Niikura ◽  
Saori Nakajima ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Functional Properties ◽  
Centric Diatom ◽  
Chaetoceros Gracilis ◽  
Extrinsic Proteins ◽  
Oxygen Evolving

Cloning, Expression of the psbU Gene, and Functional Studies of the Recombinant 12-kDa Protein of Photosystem II from a Red Alga Cyanidium caldarium

1999 ◽  
Vol 260 (1) ◽  
pp. 245-250 ◽  
Author(s):  
Hisataka Ohta ◽  
Akinori Okumura ◽  
Satoshi Okuyama ◽  
Ai Akiyama ◽  
Masako Iwai ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Red Alga ◽  
Cyanidium Caldarium ◽  
Functional Studies

scholarly journals Organisation of Photosystem I and Photosystem II in red alga Cyanidium caldarium: Encounter of cyanobacterial and higher plant concepts

2007 ◽  
Vol 1767 (6) ◽  
pp. 725-731 ◽  
Author(s):  
Zdenko Gardian ◽  
Ladislav Bumba ◽  
Adam Schrofel ◽  
Miroslava Herbstova ◽  
Jana Nebesarova ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Photosystem I ◽  
Red Alga ◽  
Cyanidium Caldarium ◽  
Higher Plant

Purification And Crystallization Of Photosystem Ii Dimer Complex From A Red Alga Cyanidium Caldarium

2008 ◽  
pp. 353-356
Author(s):  
Hideyuki Adachi ◽  
Isao Enami ◽  
Takahiro Henmi ◽  
Nobuo Kamiya ◽  
Jian-Ren Shen
Keyword(s):  
Photosystem Ii ◽  
Red Alga ◽  
Cyanidium Caldarium

scholarly journals A Reaction Center-dependent Photoprotection Mechanism in a Highly Robust Photosystem II from an Extremophilic Red Alga,Cyanidioschyzon merolae

2013 ◽  
Vol 288 (32) ◽  
pp. 23529-23542 ◽  
Author(s):  
Tomasz Krupnik ◽  
Eva Kotabová ◽  
Laura S. van Bezouwen ◽  
Radosław Mazur ◽  
Maciej Garstka ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Reaction Center ◽  
Red Alga ◽  
Cyanidioschyzon Merolae

scholarly journals Evidence that D1 Processing Is Required for Manganese Binding and Extrinsic Protein Assembly into Photosystem II

2004 ◽  
Vol 279 (44) ◽  
pp. 45417-45422 ◽  
Author(s):  
Johnna L. Roose ◽  
Himadri B. Pakrasi
Keyword(s):  
Photosystem Ii ◽  
Mutant Cell ◽  
Protein A ◽  
D1 Protein ◽  
Fluorescence Decay ◽  
Normal Function ◽  
Temporal Position ◽  
Decay Kinetics ◽  
Fluorescence Decay Kinetics ◽  
Extrinsic Proteins

Photosystem II (PSII) is a large membrane protein complex that catalyzes oxidation of water to molecular oxygen. During its normal function, PSII is damaged and frequently turned over. The maturation of the D1 protein, a key component in PSII, is a critical step in PSII biogenesis. The precursor form of D1 (pD1) contains a C-terminal extension, which is removed by the protease CtpA to yield PSII complexes with oxygen evolution activity. To determine the temporal position of D1 processing in the PSII assembly pathway, PSII complexes containing only pD1 were isolated from a CtpA-deficient strain of the cyanobacteriumSynechocystis6803. Although membranes from the mutant cell had nearly 50% manganese, no manganese was detected in isolated ΔctpAHT3 PSII, indicating a severely decreased manganese affinity. However, chlorophyll fluorescence decay kinetics after a single saturating flash suggested that the donor YZwas accessible to exogenous Mn2+ions. Furthermore, the extrinsic proteins PsbO, PsbU, and PsbV were not present in PSII isolated from this mutant. However, PsbO and PsbV were present in mutant membranes, but the amount of PsbV protein was consistently less in the mutant membranes compared with the control membranes. We conclude that D1 processing precedes manganese binding and assembly of the extrinsic proteins into PSII. Interestingly, the Psb27 protein was found to be more abundant in ΔctpAHT3 PSII than in HT3 PSII, suggesting a possible role of Psb27 as an assembly factor during PSII biogenesis.

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