Assembly of D1/D2 complexes of photosystem II: Binding of pigments and a network of auxiliary proteins
Chlorophyll
570
SP PCC 6803
high-light
Plant Biology & Botany
SYNECHOCYSTIS SP PCC-6803
07 Agricultural and Veterinary Sciences
chlorophyll
CRYSTAL-STRUCTURE
ELECTRON-TRANSPORT
Research Articles
synechocystis sp pcc-6803
mutants
580
REPAIR
photosynthesis
Science & Technology
EARLY STEPS
HIGH-LIGHT
Photosystem I Protein Complex
PHOTOSYNTHESIS
Plant Sciences
Pheophytins
Synechocystis
crystal-structure
Photosystem II Protein Complex
06 Biological Sciences
CHLOROPHYLL
electron-transport
MUTANTS
sp pcc 6803
early steps
repair
Life Sciences & Biomedicine
DOI:
10.1093/plphys/kiac045
Publication Date:
2022-01-29T20:09:03Z
AUTHORS (10)
ABSTRACT
Abstract Photosystem II (PSII) is the multi-subunit light-driven oxidoreductase that drives photosynthetic electron transport using electrons extracted from water. To investigate initial steps of PSII assembly, we used strains cyanobacterium Synechocystis sp. PCC 6803 arrested at early stages biogenesis and expressing affinity-tagged subunits to isolate reaction center assembly (RCII) complexes their precursor D1 D2 modules (D1mod D2mod). RCII preparations isolated either a His-tagged or FLAG-tagged PsbI subunit contained previously described RCIIa RCII* differ with respect presence Ycf39 factor high light-inducible proteins (Hlips) larger complex consisting bound monomeric PSI. All D1, D2, PsbI, PsbE, PsbF factors rubredoxin A Ycf48, but also detected PsbN, Slr1470, Slr0575 proteins, which all have plant homologs. The prohibitins/stomatins (Phbs) unknown function FtsH protease subunits. were active in light-induced primary charge separation chlorophylls (Chls), pheophytins, beta-carotenes, heme. D1mod consisted D1/PsbI/Ycf48 some Phb3, while D2mod D2/cytochrome b559 co-purifying PsbY, Phb1, FtsH2/FtsH3, CyanoP, Slr1470. As stably bound, Chl was not D2mod, formation appears be important for stable binding most Chls both pheophytins. We suggest can delivered I Ycf39/Hlips complexes.
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