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Plant LHC-like proteins show robust folding and static non-photochemical quenching
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SYSNO ASEP 0549716 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Plant LHC-like proteins show robust folding and static non-photochemical quenching Author(s) Skotnicová, Petra (MBU-M) ORCID, RID
Staleva-Musto, H. (CZ)
Kuznetsova, V. (CZ)
Bína, David (BC-A) RID, ORCID
Konert, Minna Maria (MBU-M)
Lu, S. (CN)
Polívka, Tomáš (BC-A) RID, ORCID
Sobotka, Roman (MBU-M) RID, ORCIDArticle number 6890 Source Title Nature Communications. - : Nature Publishing Group
Roč. 12, č. 1 (2021)Number of pages 10 s. Language eng - English Country DE - Germany Keywords light-harvesting-complex ; chlorophyll-a/b-complex ; inducible proteins ; bind chlorophyll ; pcc 6803 ; arabidopsis ; lil3 ; xanthophylls ; carotenoids ; energy Subject RIV EE - Microbiology, Virology OECD category Microbiology Subject RIV - cooperation Biology Centre (since 2006) - Biochemistry Method of publishing Open access Institutional support MBU-M - RVO:61388971 ; BC-A - RVO:60077344 UT WOS 000722866700026 EID SCOPUS 85119865478 DOI 10.1038/s41467-021-27155-1 Annotation 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.Workplace Institute of Microbiology Contact Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Year of Publishing 2022 Electronic address https://www.nature.com/articles/s41467-021-27155-1
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