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Proteomics Analysis Reveals Non-Controlled Activation of Photosynthesis and Protein Synthesis in a Rice npp1 Mutant under High Temperature and Elevated CO(2) Conditions
Rice nucleotide pyrophosphatase/phosphodiesterase 1 (NPP1) catalyzes the hydrolytic breakdown of the pyrophosphate and phosphodiester bonds of a number of nucleotides including ADP-glucose and ATP. Under high temperature and elevated CO(2) conditions (HT + ECO(2)), the npp1 knockout rice mutant disp...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6165220/ https://www.ncbi.nlm.nih.gov/pubmed/30205448 http://dx.doi.org/10.3390/ijms19092655 |
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author | Inomata, Takuya Baslam, Marouane Masui, Takahiro Koshu, Tsutomu Takamatsu, Takeshi Kaneko, Kentaro Pozueta-Romero, Javier Mitsui, Toshiaki |
author_facet | Inomata, Takuya Baslam, Marouane Masui, Takahiro Koshu, Tsutomu Takamatsu, Takeshi Kaneko, Kentaro Pozueta-Romero, Javier Mitsui, Toshiaki |
author_sort | Inomata, Takuya |
collection | PubMed |
description | Rice nucleotide pyrophosphatase/phosphodiesterase 1 (NPP1) catalyzes the hydrolytic breakdown of the pyrophosphate and phosphodiester bonds of a number of nucleotides including ADP-glucose and ATP. Under high temperature and elevated CO(2) conditions (HT + ECO(2)), the npp1 knockout rice mutant displayed rapid growth and high starch content phenotypes, indicating that NPP1 exerts a negative effect on starch accumulation and growth. To gain further insight into the mechanisms involved in the NPP1 downregulation induced starch overaccumulation, in this study we conducted photosynthesis, leaf proteomic, and chloroplast phosphoproteomic analyses of wild-type (WT) and npp1 plants cultured under HT + ECO(2). Photosynthesis in npp1 leaves was significantly higher than in WT. Additionally, npp1 leaves accumulated higher levels of sucrose than WT. The proteomic analyses revealed upregulation of proteins related to carbohydrate metabolism and the protein synthesis system in npp1 plants. Further, our data indicate the induction of 14-3-3 proteins in npp1 plants. Our finding demonstrates a higher level of protein phosphorylation in npp1 chloroplasts, which may play an important role in carbohydrate accumulation. Together, these results offer novel targets and provide additional insights into carbohydrate metabolism regulation under ambient and adverse conditions. |
format | Online Article Text |
id | pubmed-6165220 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-61652202018-10-10 Proteomics Analysis Reveals Non-Controlled Activation of Photosynthesis and Protein Synthesis in a Rice npp1 Mutant under High Temperature and Elevated CO(2) Conditions Inomata, Takuya Baslam, Marouane Masui, Takahiro Koshu, Tsutomu Takamatsu, Takeshi Kaneko, Kentaro Pozueta-Romero, Javier Mitsui, Toshiaki Int J Mol Sci Article Rice nucleotide pyrophosphatase/phosphodiesterase 1 (NPP1) catalyzes the hydrolytic breakdown of the pyrophosphate and phosphodiester bonds of a number of nucleotides including ADP-glucose and ATP. Under high temperature and elevated CO(2) conditions (HT + ECO(2)), the npp1 knockout rice mutant displayed rapid growth and high starch content phenotypes, indicating that NPP1 exerts a negative effect on starch accumulation and growth. To gain further insight into the mechanisms involved in the NPP1 downregulation induced starch overaccumulation, in this study we conducted photosynthesis, leaf proteomic, and chloroplast phosphoproteomic analyses of wild-type (WT) and npp1 plants cultured under HT + ECO(2). Photosynthesis in npp1 leaves was significantly higher than in WT. Additionally, npp1 leaves accumulated higher levels of sucrose than WT. The proteomic analyses revealed upregulation of proteins related to carbohydrate metabolism and the protein synthesis system in npp1 plants. Further, our data indicate the induction of 14-3-3 proteins in npp1 plants. Our finding demonstrates a higher level of protein phosphorylation in npp1 chloroplasts, which may play an important role in carbohydrate accumulation. Together, these results offer novel targets and provide additional insights into carbohydrate metabolism regulation under ambient and adverse conditions. MDPI 2018-09-07 /pmc/articles/PMC6165220/ /pubmed/30205448 http://dx.doi.org/10.3390/ijms19092655 Text en © 2018 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Inomata, Takuya Baslam, Marouane Masui, Takahiro Koshu, Tsutomu Takamatsu, Takeshi Kaneko, Kentaro Pozueta-Romero, Javier Mitsui, Toshiaki Proteomics Analysis Reveals Non-Controlled Activation of Photosynthesis and Protein Synthesis in a Rice npp1 Mutant under High Temperature and Elevated CO(2) Conditions |
title | Proteomics Analysis Reveals Non-Controlled Activation of Photosynthesis and Protein Synthesis in a Rice npp1 Mutant under High Temperature and Elevated CO(2) Conditions |
title_full | Proteomics Analysis Reveals Non-Controlled Activation of Photosynthesis and Protein Synthesis in a Rice npp1 Mutant under High Temperature and Elevated CO(2) Conditions |
title_fullStr | Proteomics Analysis Reveals Non-Controlled Activation of Photosynthesis and Protein Synthesis in a Rice npp1 Mutant under High Temperature and Elevated CO(2) Conditions |
title_full_unstemmed | Proteomics Analysis Reveals Non-Controlled Activation of Photosynthesis and Protein Synthesis in a Rice npp1 Mutant under High Temperature and Elevated CO(2) Conditions |
title_short | Proteomics Analysis Reveals Non-Controlled Activation of Photosynthesis and Protein Synthesis in a Rice npp1 Mutant under High Temperature and Elevated CO(2) Conditions |
title_sort | proteomics analysis reveals non-controlled activation of photosynthesis and protein synthesis in a rice npp1 mutant under high temperature and elevated co(2) conditions |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6165220/ https://www.ncbi.nlm.nih.gov/pubmed/30205448 http://dx.doi.org/10.3390/ijms19092655 |
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