Assembly of D1/D2 complexes of photosystem II: Binding of pigments and a network of auxiliary proteins
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F22%3A00558557" target="_blank" >RIV/60077344:_____/22:00558557 - isvavai.cz</a>
Alternative codes found
RIV/61388971:_____/22:00558557 RIV/60076658:12310/22:43904981
Result on the web
<a href="https://academic.oup.com/plphys/article/189/2/790/6521047?login=true" target="_blank" >https://academic.oup.com/plphys/article/189/2/790/6521047?login=true</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1093/plphys/kiac045" target="_blank" >10.1093/plphys/kiac045</a>
Alternative languages
Result language
angličtina
Original language name
Assembly of D1/D2 complexes of photosystem II: Binding of pigments and a network of auxiliary proteins
Original language description
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.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10610 - Biophysics
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2022
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Plant Physiology
ISSN
0032-0889
e-ISSN
1532-2548
Volume of the periodical
189
Issue of the periodical within the volume
2
Country of publishing house
US - UNITED STATES
Number of pages
15
Pages from-to
790-804
UT code for WoS article
000764158300001
EID of the result in the Scopus database
2-s2.0-85127044266