Structural insights into NDH-1 mediated cyclic electron transfer
NDH-1 is a key component of the cyclic-electron-transfer around photosystem I (PSI CET) pathway, an important antioxidant mechanism for efficient photosynthesis. Here, we report a 3.2-Å-resolution cryo-EM structure of the ferredoxin (Fd)-NDH-1L complex from the cyanobacterium Thermosynechococcus elo...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Nature Publishing Group UK
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7021789/ https://www.ncbi.nlm.nih.gov/pubmed/32060291 http://dx.doi.org/10.1038/s41467-020-14732-z |
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author | Zhang, Chunli Shuai, Jin Ran, Zhaoxing Zhao, Jiaohong Wu, Zhenfang Liao, Rijing Wu, Jian Ma, Weimin Lei, Ming |
author_facet | Zhang, Chunli Shuai, Jin Ran, Zhaoxing Zhao, Jiaohong Wu, Zhenfang Liao, Rijing Wu, Jian Ma, Weimin Lei, Ming |
author_sort | Zhang, Chunli |
collection | PubMed |
description | NDH-1 is a key component of the cyclic-electron-transfer around photosystem I (PSI CET) pathway, an important antioxidant mechanism for efficient photosynthesis. Here, we report a 3.2-Å-resolution cryo-EM structure of the ferredoxin (Fd)-NDH-1L complex from the cyanobacterium Thermosynechococcus elongatus. The structure reveals three β-carotene and fifteen lipid molecules in the membrane arm of NDH-1L. Regulatory oxygenic photosynthesis-specific (OPS) subunits NdhV, NdhS and NdhO are close to the Fd-binding site whilst NdhL is adjacent to the plastoquinone (PQ) cavity, and they play different roles in PSI CET under high-light stress. NdhV assists in the binding of Fd to NDH-1L and accelerates PSI CET in response to short-term high-light exposure. In contrast, prolonged high-light irradiation switches on the expression and assembly of the NDH-1MS complex, which likely contains no NdhO to further accelerate PSI CET and reduce ROS production. We propose that this hierarchical mechanism is necessary for the survival of cyanobacteria in an aerobic environment. |
format | Online Article Text |
id | pubmed-7021789 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-70217892020-02-21 Structural insights into NDH-1 mediated cyclic electron transfer Zhang, Chunli Shuai, Jin Ran, Zhaoxing Zhao, Jiaohong Wu, Zhenfang Liao, Rijing Wu, Jian Ma, Weimin Lei, Ming Nat Commun Article NDH-1 is a key component of the cyclic-electron-transfer around photosystem I (PSI CET) pathway, an important antioxidant mechanism for efficient photosynthesis. Here, we report a 3.2-Å-resolution cryo-EM structure of the ferredoxin (Fd)-NDH-1L complex from the cyanobacterium Thermosynechococcus elongatus. The structure reveals three β-carotene and fifteen lipid molecules in the membrane arm of NDH-1L. Regulatory oxygenic photosynthesis-specific (OPS) subunits NdhV, NdhS and NdhO are close to the Fd-binding site whilst NdhL is adjacent to the plastoquinone (PQ) cavity, and they play different roles in PSI CET under high-light stress. NdhV assists in the binding of Fd to NDH-1L and accelerates PSI CET in response to short-term high-light exposure. In contrast, prolonged high-light irradiation switches on the expression and assembly of the NDH-1MS complex, which likely contains no NdhO to further accelerate PSI CET and reduce ROS production. We propose that this hierarchical mechanism is necessary for the survival of cyanobacteria in an aerobic environment. Nature Publishing Group UK 2020-02-14 /pmc/articles/PMC7021789/ /pubmed/32060291 http://dx.doi.org/10.1038/s41467-020-14732-z Text en © The Author(s) 2020 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 Zhang, Chunli Shuai, Jin Ran, Zhaoxing Zhao, Jiaohong Wu, Zhenfang Liao, Rijing Wu, Jian Ma, Weimin Lei, Ming Structural insights into NDH-1 mediated cyclic electron transfer |
title | Structural insights into NDH-1 mediated cyclic electron transfer |
title_full | Structural insights into NDH-1 mediated cyclic electron transfer |
title_fullStr | Structural insights into NDH-1 mediated cyclic electron transfer |
title_full_unstemmed | Structural insights into NDH-1 mediated cyclic electron transfer |
title_short | Structural insights into NDH-1 mediated cyclic electron transfer |
title_sort | structural insights into ndh-1 mediated cyclic electron transfer |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7021789/ https://www.ncbi.nlm.nih.gov/pubmed/32060291 http://dx.doi.org/10.1038/s41467-020-14732-z |
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