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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...

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Autores principales: Inomata, Takuya, Baslam, Marouane, Masui, Takahiro, Koshu, Tsutomu, Takamatsu, Takeshi, Kaneko, Kentaro, Pozueta-Romero, Javier, Mitsui, Toshiaki
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2018
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.
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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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