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Carboxysome encapsulation of the CO(2)-fixing enzyme Rubisco in tobacco chloroplasts
A long-term strategy to enhance global crop photosynthesis and yield involves the introduction of cyanobacterial CO(2)-concentrating mechanisms (CCMs) into plant chloroplasts. Cyanobacterial CCMs enable relatively rapid CO(2) fixation by elevating intracellular inorganic carbon as bicarbonate, then...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6120970/ https://www.ncbi.nlm.nih.gov/pubmed/30177711 http://dx.doi.org/10.1038/s41467-018-06044-0 |
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author | Long, Benedict M. Hee, Wei Yih Sharwood, Robert E. Rae, Benjamin D. Kaines, Sarah Lim, Yi-Leen Nguyen, Nghiem D. Massey, Baxter Bala, Soumi von Caemmerer, Susanne Badger, Murray R. Price, G. Dean |
author_facet | Long, Benedict M. Hee, Wei Yih Sharwood, Robert E. Rae, Benjamin D. Kaines, Sarah Lim, Yi-Leen Nguyen, Nghiem D. Massey, Baxter Bala, Soumi von Caemmerer, Susanne Badger, Murray R. Price, G. Dean |
author_sort | Long, Benedict M. |
collection | PubMed |
description | A long-term strategy to enhance global crop photosynthesis and yield involves the introduction of cyanobacterial CO(2)-concentrating mechanisms (CCMs) into plant chloroplasts. Cyanobacterial CCMs enable relatively rapid CO(2) fixation by elevating intracellular inorganic carbon as bicarbonate, then concentrating it as CO(2) around the enzyme Rubisco in specialized protein micro-compartments called carboxysomes. To date, chloroplastic expression of carboxysomes has been elusive, requiring coordinated expression of almost a dozen proteins. Here we successfully produce simplified carboxysomes, isometric with those of the source organism Cyanobium, within tobacco chloroplasts. We replace the endogenous Rubisco large subunit gene with cyanobacterial Form-1A Rubisco large and small subunit genes, along with genes for two key α-carboxysome structural proteins. This minimal gene set produces carboxysomes, which encapsulate the introduced Rubisco and enable autotrophic growth at elevated CO(2). This result demonstrates the formation of α-carboxysomes from a reduced gene set, informing the step-wise construction of fully functional α-carboxysomes in chloroplasts. |
format | Online Article Text |
id | pubmed-6120970 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-61209702018-09-05 Carboxysome encapsulation of the CO(2)-fixing enzyme Rubisco in tobacco chloroplasts Long, Benedict M. Hee, Wei Yih Sharwood, Robert E. Rae, Benjamin D. Kaines, Sarah Lim, Yi-Leen Nguyen, Nghiem D. Massey, Baxter Bala, Soumi von Caemmerer, Susanne Badger, Murray R. Price, G. Dean Nat Commun Article A long-term strategy to enhance global crop photosynthesis and yield involves the introduction of cyanobacterial CO(2)-concentrating mechanisms (CCMs) into plant chloroplasts. Cyanobacterial CCMs enable relatively rapid CO(2) fixation by elevating intracellular inorganic carbon as bicarbonate, then concentrating it as CO(2) around the enzyme Rubisco in specialized protein micro-compartments called carboxysomes. To date, chloroplastic expression of carboxysomes has been elusive, requiring coordinated expression of almost a dozen proteins. Here we successfully produce simplified carboxysomes, isometric with those of the source organism Cyanobium, within tobacco chloroplasts. We replace the endogenous Rubisco large subunit gene with cyanobacterial Form-1A Rubisco large and small subunit genes, along with genes for two key α-carboxysome structural proteins. This minimal gene set produces carboxysomes, which encapsulate the introduced Rubisco and enable autotrophic growth at elevated CO(2). This result demonstrates the formation of α-carboxysomes from a reduced gene set, informing the step-wise construction of fully functional α-carboxysomes in chloroplasts. Nature Publishing Group UK 2018-09-03 /pmc/articles/PMC6120970/ /pubmed/30177711 http://dx.doi.org/10.1038/s41467-018-06044-0 Text en © The Author(s) 2018 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 Long, Benedict M. Hee, Wei Yih Sharwood, Robert E. Rae, Benjamin D. Kaines, Sarah Lim, Yi-Leen Nguyen, Nghiem D. Massey, Baxter Bala, Soumi von Caemmerer, Susanne Badger, Murray R. Price, G. Dean Carboxysome encapsulation of the CO(2)-fixing enzyme Rubisco in tobacco chloroplasts |
title | Carboxysome encapsulation of the CO(2)-fixing enzyme Rubisco in tobacco chloroplasts |
title_full | Carboxysome encapsulation of the CO(2)-fixing enzyme Rubisco in tobacco chloroplasts |
title_fullStr | Carboxysome encapsulation of the CO(2)-fixing enzyme Rubisco in tobacco chloroplasts |
title_full_unstemmed | Carboxysome encapsulation of the CO(2)-fixing enzyme Rubisco in tobacco chloroplasts |
title_short | Carboxysome encapsulation of the CO(2)-fixing enzyme Rubisco in tobacco chloroplasts |
title_sort | carboxysome encapsulation of the co(2)-fixing enzyme rubisco in tobacco chloroplasts |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6120970/ https://www.ncbi.nlm.nih.gov/pubmed/30177711 http://dx.doi.org/10.1038/s41467-018-06044-0 |
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