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...

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Autores principales: Zhang, Chunli, Shuai, Jin, Ran, Zhaoxing, Zhao, Jiaohong, Wu, Zhenfang, Liao, Rijing, Wu, Jian, Ma, Weimin, Lei, Ming
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2020
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.
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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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