Plant LHC-like proteins show robust folding and static non-photochemical quenching

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F21%3A43903232" target="_blank" >RIV/60076658:12310/21:43903232 - isvavai.cz</a>

Alternative codes found

RIV/60077344:_____/21:00549716 RIV/61388971:_____/21:00549716

Result on the web

<a href="https://www.nature.com/articles/s41467-021-27155-1.pdf" target="_blank" >https://www.nature.com/articles/s41467-021-27155-1.pdf</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1038/s41467-021-27155-1" target="_blank" >10.1038/s41467-021-27155-1</a>

Result language

angličtina

Original language name

Plant LHC-like proteins show robust folding and static non-photochemical quenching

Original language description

Plant light harvesting complex (LHC)-like proteins protect the photosynthetic machinery from excess light. Here the authors show that plant LHC-like dimers are stabilized by associated pigments and can quench chlorophyll fluorescence via direct energy transfer from chlorophyll to zeaxanthin. Life on Earth depends on photosynthesis, the conversion of light energy into chemical energy. Plants collect photons by light harvesting complexes (LHC)-abundant membrane proteins containing chlorophyll and xanthophyll molecules. LHC-like proteins are similar in their amino acid sequence to true LHC antennae, however, they rather serve a photoprotective function. Whether the LHC-like proteins bind pigments has remained unclear. Here, we characterize plant LHC-like proteins (LIL3 and ELIP2) produced in the cyanobacterium Synechocystis sp. PCC 6803 (hereafter Synechocystis). Both proteins were associated with chlorophyll a (Chl) and zeaxanthin and LIL3 was shown to be capable of quenching Chl fluorescence via direct energy transfer from the Chl Q(y) state to zeaxanthin S-1 state. Interestingly, the ability of the ELIP2 protein to quench can be acquired by modifying its N-terminal sequence. By employing Synechocystis carotenoid mutants and site-directed mutagenesis we demonstrate that, although LIL3 does not need pigments for folding, pigments stabilize the LIL3 dimer.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10301 - Atomic, molecular and chemical physics (physics of atoms and molecules including collision, interaction with radiation, magnetic resonances, Mössbauer effect)

Project

<a href="/en/project/GX19-28323X" target="_blank" >GX19-28323X: Relation between structure and function of carotenoids: New pathways to answer unresolved questions</a><br>

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2021

Confidentiality

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

Name of the periodical

Nature Communications

ISSN

2041-1723

e-ISSN

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Volume of the periodical

12

Issue of the periodical within the volume

1

Country of publishing house

DE - GERMANY

Number of pages

10

Pages from-to

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UT code for WoS article

000722866700026

EID of the result in the Scopus database

2-s2.0-85119865478