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A new, unquenched intermediate of LHCII

When plants are exposed to high-light conditions, the potentially harmful excess energy is dissipated as heat, a process called non-photochemical quenching. Efficient energy dissipation can also be induced in the major light-harvesting complex of photosystem II (LHCII) in vitro, by altering the stru...

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Autores principales: Li, Fei, Liu, Cheng, Streckaite, Simona, Yang, Chunhong, Xu, Pengqi, Llansola-Portoles, Manuel J., Ilioaia, Cristian, Pascal, Andrew A., Croce, Roberta, Robert, Bruno
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Biochemistry and Molecular Biology 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7949128/
https://www.ncbi.nlm.nih.gov/pubmed/33493515
http://dx.doi.org/10.1016/j.jbc.2021.100322
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author Li, Fei
Liu, Cheng
Streckaite, Simona
Yang, Chunhong
Xu, Pengqi
Llansola-Portoles, Manuel J.
Ilioaia, Cristian
Pascal, Andrew A.
Croce, Roberta
Robert, Bruno
author_facet Li, Fei
Liu, Cheng
Streckaite, Simona
Yang, Chunhong
Xu, Pengqi
Llansola-Portoles, Manuel J.
Ilioaia, Cristian
Pascal, Andrew A.
Croce, Roberta
Robert, Bruno
author_sort Li, Fei
collection PubMed
description When plants are exposed to high-light conditions, the potentially harmful excess energy is dissipated as heat, a process called non-photochemical quenching. Efficient energy dissipation can also be induced in the major light-harvesting complex of photosystem II (LHCII) in vitro, by altering the structure and interactions of several bound cofactors. In both cases, the extent of quenching has been correlated with conformational changes (twisting) affecting two bound carotenoids, neoxanthin, and one of the two luteins (in site L1). This lutein is directly involved in the quenching process, whereas neoxanthin senses the overall change in state without playing a direct role in energy dissipation. Here we describe the isolation of an intermediate state of LHCII, using the detergent n-dodecyl-α-D-maltoside, which exhibits the twisting of neoxanthin (along with changes in chlorophyll–protein interactions), in the absence of the L1 change or corresponding quenching. We demonstrate that neoxanthin is actually a reporter of the LHCII environment—probably reflecting a large-scale conformational change in the protein—whereas the appearance of excitation energy quenching is concomitant with the configuration change of the L1 carotenoid only, reflecting changes on a smaller scale. This unquenched LHCII intermediate, described here for the first time, provides for a deeper understanding of the molecular mechanism of quenching.
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spelling pubmed-79491282021-03-19 A new, unquenched intermediate of LHCII Li, Fei Liu, Cheng Streckaite, Simona Yang, Chunhong Xu, Pengqi Llansola-Portoles, Manuel J. Ilioaia, Cristian Pascal, Andrew A. Croce, Roberta Robert, Bruno J Biol Chem Research Article When plants are exposed to high-light conditions, the potentially harmful excess energy is dissipated as heat, a process called non-photochemical quenching. Efficient energy dissipation can also be induced in the major light-harvesting complex of photosystem II (LHCII) in vitro, by altering the structure and interactions of several bound cofactors. In both cases, the extent of quenching has been correlated with conformational changes (twisting) affecting two bound carotenoids, neoxanthin, and one of the two luteins (in site L1). This lutein is directly involved in the quenching process, whereas neoxanthin senses the overall change in state without playing a direct role in energy dissipation. Here we describe the isolation of an intermediate state of LHCII, using the detergent n-dodecyl-α-D-maltoside, which exhibits the twisting of neoxanthin (along with changes in chlorophyll–protein interactions), in the absence of the L1 change or corresponding quenching. We demonstrate that neoxanthin is actually a reporter of the LHCII environment—probably reflecting a large-scale conformational change in the protein—whereas the appearance of excitation energy quenching is concomitant with the configuration change of the L1 carotenoid only, reflecting changes on a smaller scale. This unquenched LHCII intermediate, described here for the first time, provides for a deeper understanding of the molecular mechanism of quenching. American Society for Biochemistry and Molecular Biology 2021-01-23 /pmc/articles/PMC7949128/ /pubmed/33493515 http://dx.doi.org/10.1016/j.jbc.2021.100322 Text en © 2021 The Authors https://creativecommons.org/licenses/by/4.0/This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Research Article
Li, Fei
Liu, Cheng
Streckaite, Simona
Yang, Chunhong
Xu, Pengqi
Llansola-Portoles, Manuel J.
Ilioaia, Cristian
Pascal, Andrew A.
Croce, Roberta
Robert, Bruno
A new, unquenched intermediate of LHCII
title A new, unquenched intermediate of LHCII
title_full A new, unquenched intermediate of LHCII
title_fullStr A new, unquenched intermediate of LHCII
title_full_unstemmed A new, unquenched intermediate of LHCII
title_short A new, unquenched intermediate of LHCII
title_sort new, unquenched intermediate of lhcii
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7949128/
https://www.ncbi.nlm.nih.gov/pubmed/33493515
http://dx.doi.org/10.1016/j.jbc.2021.100322
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