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Lhcx proteins provide photoprotection via thermal dissipation of absorbed light in the diatom Phaeodactylum tricornutum

Diatoms possess an impressive capacity for rapidly inducible thermal dissipation of excess absorbed energy (qE), provided by the xanthophyll diatoxanthin and Lhcx proteins. By knocking out the Lhcx1 and Lhcx2 genes individually in Phaeodactylum tricornutum strain 4 and complementing the knockout lin...

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Autores principales: Buck, Jochen M., Sherman, Jonathan, Bártulos, Carolina Río, Serif, Manuel, Halder, Marc, Henkel, Jan, Falciatore, Angela, Lavaud, Johann, Gorbunov, Maxim Y., Kroth, Peter G., Falkowski, Paul G., Lepetit, Bernard
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6744471/
https://www.ncbi.nlm.nih.gov/pubmed/31519883
http://dx.doi.org/10.1038/s41467-019-12043-6
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author Buck, Jochen M.
Sherman, Jonathan
Bártulos, Carolina Río
Serif, Manuel
Halder, Marc
Henkel, Jan
Falciatore, Angela
Lavaud, Johann
Gorbunov, Maxim Y.
Kroth, Peter G.
Falkowski, Paul G.
Lepetit, Bernard
author_facet Buck, Jochen M.
Sherman, Jonathan
Bártulos, Carolina Río
Serif, Manuel
Halder, Marc
Henkel, Jan
Falciatore, Angela
Lavaud, Johann
Gorbunov, Maxim Y.
Kroth, Peter G.
Falkowski, Paul G.
Lepetit, Bernard
author_sort Buck, Jochen M.
collection PubMed
description Diatoms possess an impressive capacity for rapidly inducible thermal dissipation of excess absorbed energy (qE), provided by the xanthophyll diatoxanthin and Lhcx proteins. By knocking out the Lhcx1 and Lhcx2 genes individually in Phaeodactylum tricornutum strain 4 and complementing the knockout lines with different Lhcx proteins, multiple mutants with varying qE capacities are obtained, ranging from zero to high values. We demonstrate that qE is entirely dependent on the concerted action of diatoxanthin and Lhcx proteins, with Lhcx1, Lhcx2 and Lhcx3 having similar functions. Moreover, we establish a clear link between Lhcx1/2/3 mediated inducible thermal energy dissipation and a reduction in the functional absorption cross-section of photosystem II. This regulation of the functional absorption cross-section can be tuned by altered Lhcx protein expression in response to environmental conditions. Our results provide a holistic understanding of the rapidly inducible thermal energy dissipation process and its mechanistic implications in diatoms.
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spelling pubmed-67444712019-09-16 Lhcx proteins provide photoprotection via thermal dissipation of absorbed light in the diatom Phaeodactylum tricornutum Buck, Jochen M. Sherman, Jonathan Bártulos, Carolina Río Serif, Manuel Halder, Marc Henkel, Jan Falciatore, Angela Lavaud, Johann Gorbunov, Maxim Y. Kroth, Peter G. Falkowski, Paul G. Lepetit, Bernard Nat Commun Article Diatoms possess an impressive capacity for rapidly inducible thermal dissipation of excess absorbed energy (qE), provided by the xanthophyll diatoxanthin and Lhcx proteins. By knocking out the Lhcx1 and Lhcx2 genes individually in Phaeodactylum tricornutum strain 4 and complementing the knockout lines with different Lhcx proteins, multiple mutants with varying qE capacities are obtained, ranging from zero to high values. We demonstrate that qE is entirely dependent on the concerted action of diatoxanthin and Lhcx proteins, with Lhcx1, Lhcx2 and Lhcx3 having similar functions. Moreover, we establish a clear link between Lhcx1/2/3 mediated inducible thermal energy dissipation and a reduction in the functional absorption cross-section of photosystem II. This regulation of the functional absorption cross-section can be tuned by altered Lhcx protein expression in response to environmental conditions. Our results provide a holistic understanding of the rapidly inducible thermal energy dissipation process and its mechanistic implications in diatoms. Nature Publishing Group UK 2019-09-13 /pmc/articles/PMC6744471/ /pubmed/31519883 http://dx.doi.org/10.1038/s41467-019-12043-6 Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Buck, Jochen M.
Sherman, Jonathan
Bártulos, Carolina Río
Serif, Manuel
Halder, Marc
Henkel, Jan
Falciatore, Angela
Lavaud, Johann
Gorbunov, Maxim Y.
Kroth, Peter G.
Falkowski, Paul G.
Lepetit, Bernard
Lhcx proteins provide photoprotection via thermal dissipation of absorbed light in the diatom Phaeodactylum tricornutum
title Lhcx proteins provide photoprotection via thermal dissipation of absorbed light in the diatom Phaeodactylum tricornutum
title_full Lhcx proteins provide photoprotection via thermal dissipation of absorbed light in the diatom Phaeodactylum tricornutum
title_fullStr Lhcx proteins provide photoprotection via thermal dissipation of absorbed light in the diatom Phaeodactylum tricornutum
title_full_unstemmed Lhcx proteins provide photoprotection via thermal dissipation of absorbed light in the diatom Phaeodactylum tricornutum
title_short Lhcx proteins provide photoprotection via thermal dissipation of absorbed light in the diatom Phaeodactylum tricornutum
title_sort lhcx proteins provide photoprotection via thermal dissipation of absorbed light in the diatom phaeodactylum tricornutum
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6744471/
https://www.ncbi.nlm.nih.gov/pubmed/31519883
http://dx.doi.org/10.1038/s41467-019-12043-6
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