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An ancient metabolite damage-repair system sustains photosynthesis in plants
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is the major catalyst in the conversion of carbon dioxide into organic compounds in photosynthetic organisms. However, its activity is impaired by binding of inhibitory sugars such as xylulose-1,5-bisphosphate (XuBP), which must be detached f...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Nature Publishing Group UK
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10212915/ https://www.ncbi.nlm.nih.gov/pubmed/37230969 http://dx.doi.org/10.1038/s41467-023-38804-y |
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author | Leister, Dario Sharma, Anurag Kerber, Natalia Nägele, Thomas Reiter, Bennet Pasch, Viviana Beeh, Simon Jahns, Peter Barbato, Roberto Pribil, Mathias Rühle, Thilo |
author_facet | Leister, Dario Sharma, Anurag Kerber, Natalia Nägele, Thomas Reiter, Bennet Pasch, Viviana Beeh, Simon Jahns, Peter Barbato, Roberto Pribil, Mathias Rühle, Thilo |
author_sort | Leister, Dario |
collection | PubMed |
description | Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is the major catalyst in the conversion of carbon dioxide into organic compounds in photosynthetic organisms. However, its activity is impaired by binding of inhibitory sugars such as xylulose-1,5-bisphosphate (XuBP), which must be detached from the active sites by Rubisco activase. Here, we show that loss of two phosphatases in Arabidopsis thaliana has detrimental effects on plant growth and photosynthesis and that this effect could be reversed by introducing the XuBP phosphatase from Rhodobacter sphaeroides. Biochemical analyses revealed that the plant enzymes specifically dephosphorylate XuBP, thus allowing xylulose-5-phosphate to enter the Calvin-Benson-Bassham cycle. Our findings demonstrate the physiological importance of an ancient metabolite damage-repair system in degradation of by-products of Rubisco, and will impact efforts to optimize carbon fixation in photosynthetic organisms. |
format | Online Article Text |
id | pubmed-10212915 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-102129152023-05-27 An ancient metabolite damage-repair system sustains photosynthesis in plants Leister, Dario Sharma, Anurag Kerber, Natalia Nägele, Thomas Reiter, Bennet Pasch, Viviana Beeh, Simon Jahns, Peter Barbato, Roberto Pribil, Mathias Rühle, Thilo Nat Commun Article Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is the major catalyst in the conversion of carbon dioxide into organic compounds in photosynthetic organisms. However, its activity is impaired by binding of inhibitory sugars such as xylulose-1,5-bisphosphate (XuBP), which must be detached from the active sites by Rubisco activase. Here, we show that loss of two phosphatases in Arabidopsis thaliana has detrimental effects on plant growth and photosynthesis and that this effect could be reversed by introducing the XuBP phosphatase from Rhodobacter sphaeroides. Biochemical analyses revealed that the plant enzymes specifically dephosphorylate XuBP, thus allowing xylulose-5-phosphate to enter the Calvin-Benson-Bassham cycle. Our findings demonstrate the physiological importance of an ancient metabolite damage-repair system in degradation of by-products of Rubisco, and will impact efforts to optimize carbon fixation in photosynthetic organisms. Nature Publishing Group UK 2023-05-25 /pmc/articles/PMC10212915/ /pubmed/37230969 http://dx.doi.org/10.1038/s41467-023-38804-y Text en © The Author(s) 2023 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 Leister, Dario Sharma, Anurag Kerber, Natalia Nägele, Thomas Reiter, Bennet Pasch, Viviana Beeh, Simon Jahns, Peter Barbato, Roberto Pribil, Mathias Rühle, Thilo An ancient metabolite damage-repair system sustains photosynthesis in plants |
title | An ancient metabolite damage-repair system sustains photosynthesis in plants |
title_full | An ancient metabolite damage-repair system sustains photosynthesis in plants |
title_fullStr | An ancient metabolite damage-repair system sustains photosynthesis in plants |
title_full_unstemmed | An ancient metabolite damage-repair system sustains photosynthesis in plants |
title_short | An ancient metabolite damage-repair system sustains photosynthesis in plants |
title_sort | ancient metabolite damage-repair system sustains photosynthesis in plants |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10212915/ https://www.ncbi.nlm.nih.gov/pubmed/37230969 http://dx.doi.org/10.1038/s41467-023-38804-y |
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