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Plant LHC-like proteins show robust folding and static non-photochemical quenching
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Plant LHC-like proteins show robust folding and static non-photochemical quenching
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Journal Article
Plant LHC-like proteins show robust folding and static non-photochemical quenching
2021
Overview
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. How pigments associated with LHC-like proteins are organised and how they contribute to protein function has not yet been determined. 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.
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.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 82/1
/ 82/16
/ 82/29
/ 82/80
/ 82/83
/ Antennae
/ Arabidopsis Proteins - chemistry
/ Arabidopsis Proteins - genetics
/ Arabidopsis Proteins - metabolism
/ Chloroplast Proteins - chemistry
/ Chloroplast Proteins - genetics
/ Chloroplast Proteins - metabolism
/ Dimers
/ Folding
/ Humanities and Social Sciences
/ Mutation
/ Photons
/ Pigments
/ Proteins
/ Science
