Mechanism of photoprotection in the cyanobacterial ancestor of plant antenna proteins

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F15%3A00447354" target="_blank" >RIV/60077344:_____/15:00447354 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61388971:_____/15:00447354 RIV/60076658:12310/15:43888683

Výsledek na webu

<a href="http://dx.doi.org/10.1038/nchembio.1755" target="_blank" >http://dx.doi.org/10.1038/nchembio.1755</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1038/nchembio.1755" target="_blank" >10.1038/nchembio.1755</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Mechanism of photoprotection in the cyanobacterial ancestor of plant antenna proteins

Popis výsledku v původním jazyce

Plants collect light for photosynthesis using light-harvesting complexes (LHCs)-an array of chlorophyll proteins that are able to reversibly switch from harvesting to energy-dissipation mode to prevent damage of the photosynthetic apparatus. LHC antennae as well as other members of the LHC superfamily evolved from cyanobacterial ancestors called high light-inducible proteins (Hlips). Here, we characterized a purified Hlip family member HliD isolated from the cyanobacterium Synechocystis sp. PCC 6803. We found that the HliD binds chlorophyll-a (Chl-a) and beta-carotene and exhibits an energy-dissipative conformation. Using femtosecond spectroscopy, we demonstrated that the energy dissipation is achieved via direct energy transfer from a Chl-a Q(y) state to the beta-carotene S-1 state. We did not detect any cation of beta-carotene that would accompany Chl-a quenching. These results provide proof of principle that this quenching mechanism operates in the LHC superfamily and also shed light on the photoprotective role of Hlips and the evolution of LHC antennae.

Název v anglickém jazyce

Mechanism of photoprotection in the cyanobacterial ancestor of plant antenna proteins

Popis výsledku anglicky

Plants collect light for photosynthesis using light-harvesting complexes (LHCs)-an array of chlorophyll proteins that are able to reversibly switch from harvesting to energy-dissipation mode to prevent damage of the photosynthetic apparatus. LHC antennae as well as other members of the LHC superfamily evolved from cyanobacterial ancestors called high light-inducible proteins (Hlips). Here, we characterized a purified Hlip family member HliD isolated from the cyanobacterium Synechocystis sp. PCC 6803. We found that the HliD binds chlorophyll-a (Chl-a) and beta-carotene and exhibits an energy-dissipative conformation. Using femtosecond spectroscopy, we demonstrated that the energy dissipation is achieved via direct energy transfer from a Chl-a Q(y) state to the beta-carotene S-1 state. We did not detect any cation of beta-carotene that would accompany Chl-a quenching. These results provide proof of principle that this quenching mechanism operates in the LHC superfamily and also shed light on the photoprotective role of Hlips and the evolution of LHC antennae.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

BO - Biofyzika

OECD FORD obor

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Projekt

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

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2015

Kód důvěrnosti údajů

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

Název periodika

Nature Chemical Biology

ISSN

1552-4450

e-ISSN

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Svazek periodika

11

Číslo periodika v rámci svazku

4

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

5

Strana od-do

287-291

Kód UT WoS článku

000351666500012

EID výsledku v databázi Scopus

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