Changes in the Functional and Structural Properties of the Mn Cluster Induced by Replacing the Side Group of the C-Terminus of the D1 Protein of Photosystem II†

Biochemistry ◽  
2004 ◽  
Vol 43 (46) ◽  
pp. 14644-14652 ◽  
Author(s):  
Naoki Mizusawa ◽  
Toshihiro Yamanari ◽  
Yukihiro Kimura ◽  
Asako Ishii ◽  
Shigeaki Nakazawa ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Structural Properties ◽  
D1 Protein ◽  
Side Group ◽  
C Terminus ◽  
Mn Cluster

Synthesis and Assembly of the D1 Protein into Photosystem II:  Processing of the C-Terminus and Identification of the Initial Assembly Partners and Complexes during Photosystem II Repair†

Biochemistry ◽  
1997 ◽  
Vol 36 (20) ◽  
pp. 6178-6186 ◽  
Author(s):  
Klaas J. van Wijk ◽  
Margrit Roobol-Boza ◽  
Reetta Kettunen ◽  
Bertil Andersson ◽  
Eva-Mari Aro
Keyword(s):  
Photosystem Ii ◽  
D1 Protein ◽  
C Terminus ◽  
Photosystem Ii Repair ◽  
Initial Assembly

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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