CyanoP is Involved in the Early Steps of Photosystem II Assembly in the Cyanobacterium Synechocystis sp PCC 6803
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F16%3A43890959" target="_blank" >RIV/60076658:12310/16:43890959 - isvavai.cz</a>
Nalezeny alternativní kódy
RIV/61388971:_____/16:00470774
Výsledek na webu
<a href="https://academic.oup.com/pcp/article-lookup/doi/10.1093/pcp/pcw115" target="_blank" >https://academic.oup.com/pcp/article-lookup/doi/10.1093/pcp/pcw115</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1093/pcp/pcw115" target="_blank" >10.1093/pcp/pcw115</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
CyanoP is Involved in the Early Steps of Photosystem II Assembly in the Cyanobacterium Synechocystis sp PCC 6803
Popis výsledku v původním jazyce
Although the PSII complex is highly conserved in cyanobacteria and chloroplasts, the PsbU and PsbV subunits stabilizing the oxygen-evolving Mn4CaO5 cluster in cyanobacteria are absent in chloroplasts and have been replaced by the PsbP and PsbQ subunits. There is, however, a distant cyanobacterial homolog of PsbP, termed CyanoP, of unknown function. Here we show that CyanoP plays a role in the early stages of PSII biogenesis in Synechocystis sp. PCC 6803. CyanoP is present in the PSII reaction center assembly complex (RCII) lacking both the CP47 and CP43 modules and binds to the smaller D2 module. A small amount of larger PSII core complexes co-purifying with FLAG-tagged CyanoP indicates that CyanoP can accompany PSII on most of its assembly pathway. A role in biogenesis is supported by the accumulation of unassembled D1 precursor and impaired formation of RCII in a mutant lacking CyanoP. Interestingly, the pull-down preparations of CyanoP-FLAG from a strain lacking CP47 also contained PsbO, indicating engagement of this protein with PSII at a much earlier stage in assembly than previously assumed.
Název v anglickém jazyce
CyanoP is Involved in the Early Steps of Photosystem II Assembly in the Cyanobacterium Synechocystis sp PCC 6803
Popis výsledku anglicky
Although the PSII complex is highly conserved in cyanobacteria and chloroplasts, the PsbU and PsbV subunits stabilizing the oxygen-evolving Mn4CaO5 cluster in cyanobacteria are absent in chloroplasts and have been replaced by the PsbP and PsbQ subunits. There is, however, a distant cyanobacterial homolog of PsbP, termed CyanoP, of unknown function. Here we show that CyanoP plays a role in the early stages of PSII biogenesis in Synechocystis sp. PCC 6803. CyanoP is present in the PSII reaction center assembly complex (RCII) lacking both the CP47 and CP43 modules and binds to the smaller D2 module. A small amount of larger PSII core complexes co-purifying with FLAG-tagged CyanoP indicates that CyanoP can accompany PSII on most of its assembly pathway. A role in biogenesis is supported by the accumulation of unassembled D1 precursor and impaired formation of RCII in a mutant lacking CyanoP. Interestingly, the pull-down preparations of CyanoP-FLAG from a strain lacking CP47 also contained PsbO, indicating engagement of this protein with PSII at a much earlier stage in assembly than previously assumed.
Klasifikace
Druh
J<sub>x</sub> - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)
CEP obor
CE - Biochemie
OECD FORD obor
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Návaznosti výsledku
Projekt
Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.
Návaznosti
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Ostatní
Rok uplatnění
2016
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Plant and Cell Physiology
ISSN
0032-0781
e-ISSN
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Svazek periodika
57
Číslo periodika v rámci svazku
9
Stát vydavatele periodika
GB - Spojené království Velké Británie a Severního Irska
Počet stran výsledku
11
Strana od-do
1921-1931
Kód UT WoS článku
000384717400011
EID výsledku v databázi Scopus
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