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De-etiolation-induced protein 1 (DEIP1) mediates assembly of the cytochrome b(6)f complex in Arabidopsis
The conversion of light energy to chemical energy by photosynthesis requires the concerted action of large protein complexes in the thylakoid membrane. Recent work has provided fundamental insights into the three-dimensional structure of these complexes, but how they are assembled from hundreds of p...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9279372/ https://www.ncbi.nlm.nih.gov/pubmed/35831297 http://dx.doi.org/10.1038/s41467-022-31758-7 |
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author | Sandoval-Ibáñez, Omar Rolo, David Ghandour, Rabea Hertle, Alexander P. Armarego-Marriott, Tegan Sampathkumar, Arun Zoschke, Reimo Bock, Ralph |
author_facet | Sandoval-Ibáñez, Omar Rolo, David Ghandour, Rabea Hertle, Alexander P. Armarego-Marriott, Tegan Sampathkumar, Arun Zoschke, Reimo Bock, Ralph |
author_sort | Sandoval-Ibáñez, Omar |
collection | PubMed |
description | The conversion of light energy to chemical energy by photosynthesis requires the concerted action of large protein complexes in the thylakoid membrane. Recent work has provided fundamental insights into the three-dimensional structure of these complexes, but how they are assembled from hundreds of parts remains poorly understood. Particularly little is known about the biogenesis of the cytochrome b(6)f complex (Cytb(6)f), the redox-coupling complex that interconnects the two photosystems. Here we report the identification of a factor that guides the assembly of Cytb(6)f in thylakoids of chloroplasts. The protein, DE-ETIOLATION-INDUCED PROTEIN 1 (DEIP1), resides in the thylakoid membrane and is essential for photoautotrophic growth. Knock-out mutants show a specific loss of Cytb(6)f, and are defective in complex assembly. We demonstrate that DEIP1 interacts with the two cytochrome subunits of the complex, PetA and PetB, and mediates the assembly of intermediates in Cytb(6)f biogenesis. The identification of DEIP1 provides an entry point into the study of the assembly pathway of a crucial complex in photosynthetic electron transfer. |
format | Online Article Text |
id | pubmed-9279372 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-92793722022-07-15 De-etiolation-induced protein 1 (DEIP1) mediates assembly of the cytochrome b(6)f complex in Arabidopsis Sandoval-Ibáñez, Omar Rolo, David Ghandour, Rabea Hertle, Alexander P. Armarego-Marriott, Tegan Sampathkumar, Arun Zoschke, Reimo Bock, Ralph Nat Commun Article The conversion of light energy to chemical energy by photosynthesis requires the concerted action of large protein complexes in the thylakoid membrane. Recent work has provided fundamental insights into the three-dimensional structure of these complexes, but how they are assembled from hundreds of parts remains poorly understood. Particularly little is known about the biogenesis of the cytochrome b(6)f complex (Cytb(6)f), the redox-coupling complex that interconnects the two photosystems. Here we report the identification of a factor that guides the assembly of Cytb(6)f in thylakoids of chloroplasts. The protein, DE-ETIOLATION-INDUCED PROTEIN 1 (DEIP1), resides in the thylakoid membrane and is essential for photoautotrophic growth. Knock-out mutants show a specific loss of Cytb(6)f, and are defective in complex assembly. We demonstrate that DEIP1 interacts with the two cytochrome subunits of the complex, PetA and PetB, and mediates the assembly of intermediates in Cytb(6)f biogenesis. The identification of DEIP1 provides an entry point into the study of the assembly pathway of a crucial complex in photosynthetic electron transfer. Nature Publishing Group UK 2022-07-13 /pmc/articles/PMC9279372/ /pubmed/35831297 http://dx.doi.org/10.1038/s41467-022-31758-7 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/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/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Article Sandoval-Ibáñez, Omar Rolo, David Ghandour, Rabea Hertle, Alexander P. Armarego-Marriott, Tegan Sampathkumar, Arun Zoschke, Reimo Bock, Ralph De-etiolation-induced protein 1 (DEIP1) mediates assembly of the cytochrome b(6)f complex in Arabidopsis |
title | De-etiolation-induced protein 1 (DEIP1) mediates assembly of the cytochrome b(6)f complex in Arabidopsis |
title_full | De-etiolation-induced protein 1 (DEIP1) mediates assembly of the cytochrome b(6)f complex in Arabidopsis |
title_fullStr | De-etiolation-induced protein 1 (DEIP1) mediates assembly of the cytochrome b(6)f complex in Arabidopsis |
title_full_unstemmed | De-etiolation-induced protein 1 (DEIP1) mediates assembly of the cytochrome b(6)f complex in Arabidopsis |
title_short | De-etiolation-induced protein 1 (DEIP1) mediates assembly of the cytochrome b(6)f complex in Arabidopsis |
title_sort | de-etiolation-induced protein 1 (deip1) mediates assembly of the cytochrome b(6)f complex in arabidopsis |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9279372/ https://www.ncbi.nlm.nih.gov/pubmed/35831297 http://dx.doi.org/10.1038/s41467-022-31758-7 |
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