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

P. Skotnicová, H. Staleva-Musto, V. Kuznetsova, D. Bína, MM. Konert, S. Lu, T. Polívka, R. Sobotka

. 2021 ; 12 (1) : 6890. [pub] 20211125

Language English Country Great Britain

Document type Journal Article, Research Support, Non-U.S. Gov't

Persistent link   https://www.medvik.cz/link/bmc22003168

Grant support
854126 EC | EU Framework Programme for Research and Innovation H2020 | H2020 Priority Excellent Science | H2020 European Research Council (H2020 Excellent Science - European Research Council)
19-28323X Grantová Agentura České Republiky (Grant Agency of the Czech Republic)

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 Qy state to zeaxanthin S1 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.

References provided by Crossref.org

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$a Life on Earth depends on photosynthesis, the conversion of light energy into chemical energy. Plants collect photons by light harvesting complexes (LHC)-abundant membrane proteins containing chlorophyll and xanthophyll molecules. LHC-like proteins are similar in their amino acid sequence to true LHC antennae, however, they rather serve a photoprotective function. Whether the LHC-like proteins bind pigments has remained unclear. Here, we characterize plant LHC-like proteins (LIL3 and ELIP2) produced in the cyanobacterium Synechocystis sp. PCC 6803 (hereafter Synechocystis). Both proteins were associated with chlorophyll a (Chl) and zeaxanthin and LIL3 was shown to be capable of quenching Chl fluorescence via direct energy transfer from the Chl Qy state to zeaxanthin S1 state. Interestingly, the ability of the ELIP2 protein to quench can be acquired by modifying its N-terminal sequence. By employing Synechocystis carotenoid mutants and site-directed mutagenesis we demonstrate that, although LIL3 does not need pigments for folding, pigments stabilize the LIL3 dimer.
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$a Staleva-Musto, Hristina $u Faculty of Science, University of South Bohemia, České Budějovice, Czech Republic
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$a Konert, Minna M $u Institute of Microbiology, Academy of Sciences of the Czech Republic, Třeboň, Czech Republic
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$a Polívka, Tomáš $u Faculty of Science, University of South Bohemia, České Budějovice, Czech Republic. tpolivka@jcu.cz $u Biology Centre, Institute of Plant Molecular Biology, Academy of Sciences of the Czech Republic, České Budějovice, Czech Republic. tpolivka@jcu.cz
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$a Sobotka, Roman $u Institute of Microbiology, Academy of Sciences of the Czech Republic, Třeboň, Czech Republic. sobotka@alga.cz
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