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Dissecting the Native Architecture and Dynamics of Cyanobacterial Photosynthetic Machinery
The structural dynamics and flexibility of cell membranes play fundamental roles in the functions of the cells, i.e., signaling, energy transduction, and physiological adaptation. The cyanobacterial thylakoid membrane represents a model membrane that can conduct both oxygenic photosynthesis and resp...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5683893/ https://www.ncbi.nlm.nih.gov/pubmed/29017828 http://dx.doi.org/10.1016/j.molp.2017.09.019 |
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author | Casella, Selene Huang, Fang Mason, David Zhao, Guo-Yan Johnson, Giles N. Mullineaux, Conrad W. Liu, Lu-Ning |
author_facet | Casella, Selene Huang, Fang Mason, David Zhao, Guo-Yan Johnson, Giles N. Mullineaux, Conrad W. Liu, Lu-Ning |
author_sort | Casella, Selene |
collection | PubMed |
description | The structural dynamics and flexibility of cell membranes play fundamental roles in the functions of the cells, i.e., signaling, energy transduction, and physiological adaptation. The cyanobacterial thylakoid membrane represents a model membrane that can conduct both oxygenic photosynthesis and respiration simultaneously. In this study, we conducted direct visualization of the global organization and mobility of photosynthetic complexes in thylakoid membranes from a model cyanobacterium, Synechococcus elongatus PCC 7942, using high-resolution atomic force, confocal, and total internal reflection fluorescence microscopy. We visualized the native arrangement and dense packing of photosystem I (PSI), photosystem II (PSII), and cytochrome (Cyt) b(6)f within thylakoid membranes at the molecular level. Furthermore, we functionally tagged PSI, PSII, Cyt b(6)f, and ATP synthase individually with fluorescent proteins, and revealed the heterogeneous distribution of these four photosynthetic complexes and determined their dynamic features within the crowding membrane environment using live-cell fluorescence imaging. We characterized red light-induced clustering localization and adjustable diffusion of photosynthetic complexes in thylakoid membranes, representative of the reorganization of photosynthetic apparatus in response to environmental changes. Understanding the organization and dynamics of photosynthetic membranes is essential for rational design and construction of artificial photosynthetic systems to underpin bioenergy development. Knowledge of cyanobacterial thylakoid membranes could also be extended to other cell membranes, such as chloroplast and mitochondrial membranes. |
format | Online Article Text |
id | pubmed-5683893 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-56838932017-11-20 Dissecting the Native Architecture and Dynamics of Cyanobacterial Photosynthetic Machinery Casella, Selene Huang, Fang Mason, David Zhao, Guo-Yan Johnson, Giles N. Mullineaux, Conrad W. Liu, Lu-Ning Mol Plant Article The structural dynamics and flexibility of cell membranes play fundamental roles in the functions of the cells, i.e., signaling, energy transduction, and physiological adaptation. The cyanobacterial thylakoid membrane represents a model membrane that can conduct both oxygenic photosynthesis and respiration simultaneously. In this study, we conducted direct visualization of the global organization and mobility of photosynthetic complexes in thylakoid membranes from a model cyanobacterium, Synechococcus elongatus PCC 7942, using high-resolution atomic force, confocal, and total internal reflection fluorescence microscopy. We visualized the native arrangement and dense packing of photosystem I (PSI), photosystem II (PSII), and cytochrome (Cyt) b(6)f within thylakoid membranes at the molecular level. Furthermore, we functionally tagged PSI, PSII, Cyt b(6)f, and ATP synthase individually with fluorescent proteins, and revealed the heterogeneous distribution of these four photosynthetic complexes and determined their dynamic features within the crowding membrane environment using live-cell fluorescence imaging. We characterized red light-induced clustering localization and adjustable diffusion of photosynthetic complexes in thylakoid membranes, representative of the reorganization of photosynthetic apparatus in response to environmental changes. Understanding the organization and dynamics of photosynthetic membranes is essential for rational design and construction of artificial photosynthetic systems to underpin bioenergy development. Knowledge of cyanobacterial thylakoid membranes could also be extended to other cell membranes, such as chloroplast and mitochondrial membranes. Oxford University Press 2017-11-06 /pmc/articles/PMC5683893/ /pubmed/29017828 http://dx.doi.org/10.1016/j.molp.2017.09.019 Text en © 2017 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Casella, Selene Huang, Fang Mason, David Zhao, Guo-Yan Johnson, Giles N. Mullineaux, Conrad W. Liu, Lu-Ning Dissecting the Native Architecture and Dynamics of Cyanobacterial Photosynthetic Machinery |
title | Dissecting the Native Architecture and Dynamics of Cyanobacterial Photosynthetic Machinery |
title_full | Dissecting the Native Architecture and Dynamics of Cyanobacterial Photosynthetic Machinery |
title_fullStr | Dissecting the Native Architecture and Dynamics of Cyanobacterial Photosynthetic Machinery |
title_full_unstemmed | Dissecting the Native Architecture and Dynamics of Cyanobacterial Photosynthetic Machinery |
title_short | Dissecting the Native Architecture and Dynamics of Cyanobacterial Photosynthetic Machinery |
title_sort | dissecting the native architecture and dynamics of cyanobacterial photosynthetic machinery |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5683893/ https://www.ncbi.nlm.nih.gov/pubmed/29017828 http://dx.doi.org/10.1016/j.molp.2017.09.019 |
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