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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...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society for Biochemistry and Molecular Biology
2021
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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. |
format | Online Article Text |
id | pubmed-7949128 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | American Society for Biochemistry and Molecular Biology |
record_format | MEDLINE/PubMed |
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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