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Phosphoserine Aminotransferase1 Is Part of the Phosphorylated Pathways for Serine Biosynthesis and Essential for Light and Sugar-Dependent Growth Promotion
The phosphorylated pathway of serine biosynthesis represents an important pathway in plants. The pathway consist of three reactions catalyzed by the phosphoglycerate dehydrogenase, the phosphoserine aminotransferase and the phosphoserine phosphatase, and the genes encoding for all enzymes of the pat...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6256069/ https://www.ncbi.nlm.nih.gov/pubmed/30515188 http://dx.doi.org/10.3389/fpls.2018.01712 |
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author | Wulfert, Sabine Krueger, Stephan |
author_facet | Wulfert, Sabine Krueger, Stephan |
author_sort | Wulfert, Sabine |
collection | PubMed |
description | The phosphorylated pathway of serine biosynthesis represents an important pathway in plants. The pathway consist of three reactions catalyzed by the phosphoglycerate dehydrogenase, the phosphoserine aminotransferase and the phosphoserine phosphatase, and the genes encoding for all enzymes of the pathway have been identified. Previously, the importance of the phosphoglycerate dehydrogenase and phosphoserine phosphatase for plant metabolism and development has been shown, but due to the lack of T-DNA insertion mutants, a physiological characterization of the phosphoserine aminotransferase is still missing. Hence, we generated silencing lines specifically down-regulated in the expression of the major PSAT1 gene. The morphological characterization of the obtained PSAT1-silenced lines revealed a strong inhibition of shoot and root growth. In addition, these lines are hypersensitive to the inhibition of the photorespiratory serine biosynthesis, when growing the plants at elevated CO(2). Metabolic analysis of PSAT1-silenced lines, showed a strong accumulation of certain amino acids, most likely due to an enhanced ammonium assimilation. Furthermore, phenotypic analysis under low and high-light conditions and in the presence of sucrose revealed, that the phosphorylated pathway of serine biosynthesis is essential for light and sugar-dependent growth promotion in plants. |
format | Online Article Text |
id | pubmed-6256069 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-62560692018-12-04 Phosphoserine Aminotransferase1 Is Part of the Phosphorylated Pathways for Serine Biosynthesis and Essential for Light and Sugar-Dependent Growth Promotion Wulfert, Sabine Krueger, Stephan Front Plant Sci Plant Science The phosphorylated pathway of serine biosynthesis represents an important pathway in plants. The pathway consist of three reactions catalyzed by the phosphoglycerate dehydrogenase, the phosphoserine aminotransferase and the phosphoserine phosphatase, and the genes encoding for all enzymes of the pathway have been identified. Previously, the importance of the phosphoglycerate dehydrogenase and phosphoserine phosphatase for plant metabolism and development has been shown, but due to the lack of T-DNA insertion mutants, a physiological characterization of the phosphoserine aminotransferase is still missing. Hence, we generated silencing lines specifically down-regulated in the expression of the major PSAT1 gene. The morphological characterization of the obtained PSAT1-silenced lines revealed a strong inhibition of shoot and root growth. In addition, these lines are hypersensitive to the inhibition of the photorespiratory serine biosynthesis, when growing the plants at elevated CO(2). Metabolic analysis of PSAT1-silenced lines, showed a strong accumulation of certain amino acids, most likely due to an enhanced ammonium assimilation. Furthermore, phenotypic analysis under low and high-light conditions and in the presence of sucrose revealed, that the phosphorylated pathway of serine biosynthesis is essential for light and sugar-dependent growth promotion in plants. Frontiers Media S.A. 2018-11-20 /pmc/articles/PMC6256069/ /pubmed/30515188 http://dx.doi.org/10.3389/fpls.2018.01712 Text en Copyright © 2018 Wulfert and Krueger. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Plant Science Wulfert, Sabine Krueger, Stephan Phosphoserine Aminotransferase1 Is Part of the Phosphorylated Pathways for Serine Biosynthesis and Essential for Light and Sugar-Dependent Growth Promotion |
title | Phosphoserine Aminotransferase1 Is Part of the Phosphorylated Pathways for Serine Biosynthesis and Essential for Light and Sugar-Dependent Growth Promotion |
title_full | Phosphoserine Aminotransferase1 Is Part of the Phosphorylated Pathways for Serine Biosynthesis and Essential for Light and Sugar-Dependent Growth Promotion |
title_fullStr | Phosphoserine Aminotransferase1 Is Part of the Phosphorylated Pathways for Serine Biosynthesis and Essential for Light and Sugar-Dependent Growth Promotion |
title_full_unstemmed | Phosphoserine Aminotransferase1 Is Part of the Phosphorylated Pathways for Serine Biosynthesis and Essential for Light and Sugar-Dependent Growth Promotion |
title_short | Phosphoserine Aminotransferase1 Is Part of the Phosphorylated Pathways for Serine Biosynthesis and Essential for Light and Sugar-Dependent Growth Promotion |
title_sort | phosphoserine aminotransferase1 is part of the phosphorylated pathways for serine biosynthesis and essential for light and sugar-dependent growth promotion |
topic | Plant Science |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6256069/ https://www.ncbi.nlm.nih.gov/pubmed/30515188 http://dx.doi.org/10.3389/fpls.2018.01712 |
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