The robustness of the terminal emitter site in major LHCII complexes controls xanthophyll function during photoprotection
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F20%3A43901340" target="_blank" >RIV/60076658:12310/20:43901340 - isvavai.cz</a>
Výsledek na webu
<a href="https://pubs.rsc.org/en/content/articlelanding/2020/PP/D0PP00174K#!divAbstract" target="_blank" >https://pubs.rsc.org/en/content/articlelanding/2020/PP/D0PP00174K#!divAbstract</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1039/d0pp00174k" target="_blank" >10.1039/d0pp00174k</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
The robustness of the terminal emitter site in major LHCII complexes controls xanthophyll function during photoprotection
Popis výsledku v původním jazyce
Xanthophylls in light harvesting complexes perform a number of functions ranging from structural support to light-harvesting and photoprotection. In the major light harvesting complex of photosystem II in plants (LHCII), the innermost xanthophyll binding pockets are occupied by lutein molecules. The conservation of these sites within the LHC protein family suggests their importance in LHCII functionality. In the present work, we induced the photoprotective switch in LHCII isolated from theArabidopsismutantnpq1lut2, where the lutein molecules are exchanged with violaxanthin. Despite the differences in the energetics of the pigments and the impairment of chlorophyll fluorescence quenchingin vivo, we show that isolated complexes containing violaxanthin are still able to induce the quenching switch to a similar extent to wild type LHCII monomers. Moreover, the same spectroscopic changes take place, which suggest the involvement of the terminal emitter site (L1) in energy dissipation in both complexes. These results indicate the robust nature of the L1 xanthophyll binding domain in LHCII, where protein structural cues are the major determinant of the function of the bound carotenoid.
Název v anglickém jazyce
The robustness of the terminal emitter site in major LHCII complexes controls xanthophyll function during photoprotection
Popis výsledku anglicky
Xanthophylls in light harvesting complexes perform a number of functions ranging from structural support to light-harvesting and photoprotection. In the major light harvesting complex of photosystem II in plants (LHCII), the innermost xanthophyll binding pockets are occupied by lutein molecules. The conservation of these sites within the LHC protein family suggests their importance in LHCII functionality. In the present work, we induced the photoprotective switch in LHCII isolated from theArabidopsismutantnpq1lut2, where the lutein molecules are exchanged with violaxanthin. Despite the differences in the energetics of the pigments and the impairment of chlorophyll fluorescence quenchingin vivo, we show that isolated complexes containing violaxanthin are still able to induce the quenching switch to a similar extent to wild type LHCII monomers. Moreover, the same spectroscopic changes take place, which suggest the involvement of the terminal emitter site (L1) in energy dissipation in both complexes. These results indicate the robust nature of the L1 xanthophyll binding domain in LHCII, where protein structural cues are the major determinant of the function of the bound carotenoid.
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
10610 - Biophysics
Návaznosti výsledku
Projekt
<a href="/cs/project/GX19-28323X" target="_blank" >GX19-28323X: Vztah mezi strukturou a funkcí karotenoidů: Nové cesty k řešení nezodpovězených otázek</a><br>
Návaznosti
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Ostatní
Rok uplatnění
2020
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Photochemical & Photobiological Sciences
ISSN
1474-905X
e-ISSN
—
Svazek periodika
19
Číslo periodika v rámci svazku
10
Stát vydavatele periodika
GB - Spojené království Velké Británie a Severního Irska
Počet stran výsledku
11
Strana od-do
1308-1318
Kód UT WoS článku
000577752100006
EID výsledku v databázi Scopus
2-s2.0-85092945511