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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...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2019
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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. |
format | Online Article Text |
id | pubmed-6744471 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
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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