Assembly of D1/D2 complexes of photosystem II: Binding of pigments and a network of auxiliary proteins

Kód výsledku v 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>

Nalezeny alternativní kódy

RIV/61388971:_____/22:00558557 RIV/60076658:12310/22:43904981

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

Assembly of D1/D2 complexes of photosystem II: Binding of pigments and a network of auxiliary proteins

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

Assembly of D1/D2 complexes of photosystem II: Binding of pigments and a network of auxiliary proteins

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10610 - Biophysics

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2022

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Plant Physiology

ISSN

0032-0889

e-ISSN

1532-2548

Svazek periodika

189

Číslo periodika v rámci svazku

2

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

15

Strana od-do

790-804

Kód UT WoS článku

000764158300001

EID výsledku v databázi Scopus

2-s2.0-85127044266