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Assembly of D1/D2 complexes of photosystem II: Binding of pigments and a network of auxiliary proteins
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SYSNO ASEP 0558557 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Assembly of D1/D2 complexes of photosystem II: Binding of pigments and a network of auxiliary proteins Author(s) Knoppová, Jana (MBU-M) RID
Sobotka, Roman (MBU-M) RID, ORCID
Yu, J. (GB)
Bečková, Martina (MBU-M) RID
Pilný, Jan (MBU-M) ORCID
Trinugroho, J. (GB)
Csefalvay, Ladislav (MBU-M)
Bína, David (BC-A) RID, ORCID
Nixon, P. (GB)
Komenda, Josef (MBU-M) RID, ORCIDSource Title Plant Physiology. - : Oxford University Press - ISSN 0032-0889
Roč. 189, č. 2 (2022), s. 790-804Number of pages 15 s. Language eng - English Country US - United States Keywords synechocystis sp pcc-6803 ; sp pcc 6803 ; electron-transport ; crystal-structure ; early steps ; high-light ; chlorophyll ; repair ; mutants ; photosynthesis Subject RIV EE - Microbiology, Virology OECD category Microbiology Subject RIV - cooperation Biology Centre (since 2006) - Biophysics R&D Projects GX19-29225X GA ČR - Czech Science Foundation (CSF) EF15_003/0000336 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) Method of publishing Open access Institutional support MBU-M - RVO:61388971 ; BC-A - RVO:60077344 UT WOS 000764158300001 EID SCOPUS 85127044266 DOI 10.1093/plphys/kiac045 Annotation Analysis of isolated assembly complexes provides new insights into the early stages of photosystem II biogenesis. Photosystem II (PSII) is the multi-subunit light-driven oxidoreductase that drives photosynthetic electron transport using electrons extracted from water. To investigate the initial steps of PSII assembly, we used strains of the cyanobacterium Synechocystis sp. PCC 6803 arrested at early stages of PSII biogenesis and expressing affinity-tagged PSII subunits to isolate PSII reaction center assembly (RCII) complexes and their precursor D1 and D2 modules (D1(mod) and D2(mod)). RCII preparations isolated using either a His-tagged D2 or a FLAG-tagged PsbI subunit contained the previously described RCIIa and RCII* complexes that differ with respect to the presence of the Ycf39 assembly factor and high light-inducible proteins (Hlips) and a larger complex consisting of RCIIa bound to monomeric PSI. All RCII complexes contained the PSII subunits D1, D2, PsbI, PsbE, and PsbF and the assembly factors rubredoxin A and Ycf48, but we also detected PsbN, Slr1470, and the Slr0575 proteins, which all have plant homologs. The RCII preparations also contained prohibitins/stomatins (Phbs) of unknown function and FtsH protease subunits. RCII complexes were active in light-induced primary charge separation and bound chlorophylls (Chls), pheophytins, beta-carotenes, and heme. The isolated D1(mod) consisted of D1/PsbI/Ycf48 with some Ycf39 and Phb3, while D2(mod) contained D2/cytochrome b(559) with co-purifying PsbY, Phb1, Phb3, FtsH2/FtsH3, CyanoP, and Slr1470. As stably bound, Chl was detected in D1(mod) but not D2(mod), formation of RCII appears to be important for stable binding of most of the Chls and both pheophytins. We suggest that Chl can be delivered to RCII from either monomeric Photosystem I or Ycf39/Hlips complexes. Workplace Institute of Microbiology Contact Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Year of Publishing 2023 Electronic address https://academic.oup.com/plphys/article/189/2/790/6521047?login=true
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