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

0549716 - MBÚ 2022 RIV DE eng J - Journal Article
Skotnicová, Petra - Staleva-Musto, H. - Kuznetsova, V. - Bína, David - Konert, Minna Maria - Lu, S. - Polívka, Tomáš - Sobotka, Roman
Plant LHC-like proteins show robust folding and static non-photochemical quenching.
Nature Communications. Roč. 12, č. 1 (2021), č. článku 6890. E-ISSN 2041-1723
EU Projects: European Commission(CZ) 854126 - PhotoRedesign
Institutional support: RVO:61388971 ; RVO:60077344
Keywords : light-harvesting-complex * chlorophyll-a/b-complex * inducible proteins * bind chlorophyll * pcc 6803 * arabidopsis * lil3 * xanthophylls * carotenoids * energy
OECD category: Microbiology; Biochemistry and molecular biology (BC-A)
Impact factor: 17.694, year: 2021
Method of publishing: Open access
https://www.nature.com/articles/s41467-021-27155-1

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.
Permanent Link: http://hdl.handle.net/11104/0325655