Turnover of the D1 protein and of Photosystem II in a Synechocystis 6803 mutant lacking Tyrz

1995 ◽  
Vol 45 (2) ◽  
pp. 99-104 ◽  
Author(s):  
Wim Vermaas ◽  
Cathy Madsen ◽  
Jiujiang Yu ◽  
Janine Visser ◽  
James Metz ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
D1 Protein ◽  
Synechocystis 6803

Constructed deletions in lumen-exposed regions of the D1 protein in the cyanobacterium Synechocystis 6803: Effects on D1 insertion and accumulation in the thylakoid membrane, and on Photosystem II assembly

1996 ◽  
Vol 49 (2) ◽  
pp. 131-140 ◽  
Author(s):  
Gaza Salih ◽  
Ronney Wiklund ◽  
Taina Tyystj�rvi ◽  
Pirkko M�enp�� ◽  
Catherine Gerez ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Thylakoid Membrane ◽  
D1 Protein ◽  
Synechocystis 6803

Charge stabilization and recombination in Photosystem II containing the D1′ protein product of the psbA1 gene in Synechocystis 6803

2004 ◽  
Vol 6 (20) ◽  
pp. 4832-4837 ◽  
Author(s):  
Cosmin Sicora ◽  
Ronney Wiklund ◽  
Christer Jansson ◽  
Imre Vass
Keyword(s):  
Photosystem Ii ◽  
D1 Protein ◽  
Protein Product ◽  
Synechocystis 6803 ◽  
Charge Stabilization

Recovery of Photosystem II Activity in PhotoinhibitedSynechocystisCells:  Light-Dependent Translation Activity Is Required besides Light-Independent Synthesis of the D1 Protein†

Biochemistry ◽  
2000 ◽  
Vol 39 (8) ◽  
pp. 2032-2041 ◽  
Author(s):  
Sabine Constant ◽  
Yael Eisenberg-Domovitch ◽  
Itzhak Ohad ◽  
Diana Kirilovsky
Keyword(s):  
Photosystem Ii ◽  
D1 Protein ◽  
Independent Synthesis ◽  
Photosystem Ii Activity

Breakdown of the photosystem II reaction center D1 protein under photoinhibitory conditions: identification and localization of the C-terminal degradation products

Biochemistry ◽  
1991 ◽  
Vol 30 (42) ◽  
pp. 10220-10226 ◽  
Author(s):  
Roberto Barbato ◽  
Giulia Friso ◽  
Maria Teresa Giardi ◽  
Fernanda Rigoni ◽  
Giorgio Mario Giacometti
Keyword(s):  
Photosystem Ii ◽  
Reaction Center ◽  
Degradation Products ◽  
D1 Protein

The Thylakoid FtsH Protease Plays a Role in the Light-Induced Turnover of the Photosystem II D1 Protein

2000 ◽  
Vol 12 (3) ◽  
pp. 419 ◽  
Author(s):  
Marika Lindahl ◽  
Cornelia Spetea ◽  
Torill Hundal ◽  
Amos B. Oppenheim ◽  
Zach Adam ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
D1 Protein ◽  
Ftsh Protease

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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