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

Autor: Veronika Reisinger, Josef Komenda, Martina Bečková, Marko Boehm, Lutz A. Eichacker, Eberhard Schlodder, Peter J. Nixon, Jianfeng Yu
Rok vydání: 2012
Předmět:
0106 biological sciences
Photosystem II
Mutant
Light-Harvesting Protein Complexes
Plasma protein binding
Thylakoids
01 natural sciences
Protein Interaction Mapping
Plant Proteins
0303 health sciences
biology
Protein Stability
Synechocystis
food and beverages
P680
Articles
Photochemical Processes
Protein Transport
Biochemistry
ScpC
Thylakoid
Psb28
Electrophoresis
Polyacrylamide Gel
General Agricultural and Biological Sciences
Oxidation-Reduction
Protein Binding
Research Article
RC47
Protein subunit
macromolecular substances
General Biochemistry
Genetics and Molecular Biology
low-molecular-mass subunit
Electron Transport
03 medical and health sciences
Bacterial Proteins
030304 developmental biology
Membrane Proteins
Photosystem II Protein Complex
biology.organism_classification
Molecular Weight
Oxygen
Membrane protein
Genes
Bacterial
accessory factor
Biophysics
Holoenzymes
Gene Deletion
010606 plant biology & botany
Zdroj: Philosophical Transactions of the Royal Society B: Biological Sciences
ISSN: 1471-2970
0962-8436
DOI: 10.1098/rstb.2012.0066
Popis: 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.
Databáze: OpenAIRE
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