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Inhibition of SNF1-Related Protein Kinase1 Activity and Regulation of Metabolic Pathways by Trehalose-6-Phosphate
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| Zeitschriftentitel: | Plant Physiology |
|---|---|
| Personen und Körperschaften: | , , , , , , , , , |
| In: | Plant Physiology, 149, 2009, 4, S. 1860-1871 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Oxford University Press (OUP)
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| Schlagwörter: |
| author_facet |
Zhang, Yuhua Primavesi, Lucia F. Jhurreea, Deveraj Andralojc, P. John Mitchell, Rowan A.C. Powers, Stephen J. Schluepmann, Henriette Delatte, Thierry Wingler, Astrid Paul, Matthew J. Zhang, Yuhua Primavesi, Lucia F. Jhurreea, Deveraj Andralojc, P. John Mitchell, Rowan A.C. Powers, Stephen J. Schluepmann, Henriette Delatte, Thierry Wingler, Astrid Paul, Matthew J. |
|---|---|
| author |
Zhang, Yuhua Primavesi, Lucia F. Jhurreea, Deveraj Andralojc, P. John Mitchell, Rowan A.C. Powers, Stephen J. Schluepmann, Henriette Delatte, Thierry Wingler, Astrid Paul, Matthew J. |
| spellingShingle |
Zhang, Yuhua Primavesi, Lucia F. Jhurreea, Deveraj Andralojc, P. John Mitchell, Rowan A.C. Powers, Stephen J. Schluepmann, Henriette Delatte, Thierry Wingler, Astrid Paul, Matthew J. Plant Physiology Inhibition of SNF1-Related Protein Kinase1 Activity and Regulation of Metabolic Pathways by Trehalose-6-Phosphate Plant Science Genetics Physiology |
| author_sort |
zhang, yuhua |
| spelling |
Zhang, Yuhua Primavesi, Lucia F. Jhurreea, Deveraj Andralojc, P. John Mitchell, Rowan A.C. Powers, Stephen J. Schluepmann, Henriette Delatte, Thierry Wingler, Astrid Paul, Matthew J. 1532-2548 Oxford University Press (OUP) Plant Science Genetics Physiology http://dx.doi.org/10.1104/pp.108.133934 <jats:title>Abstract</jats:title> <jats:p>Trehalose-6-phosphate (T6P) is a proposed signaling molecule in plants, yet how it signals was not clear. Here, we provide evidence that T6P functions as an inhibitor of SNF1-related protein kinase1 (SnRK1; AKIN10/AKIN11) of the SNF1-related group of protein kinases. T6P, but not other sugars and sugar phosphates, inhibited SnRK1 in Arabidopsis (Arabidopsis thaliana) seedling extracts strongly (50%) at low concentrations (1–20 μ m). Inhibition was noncompetitive with respect to ATP. In immunoprecipitation studies using antibodies to AKIN10 and AKIN11, SnRK1 catalytic activity and T6P inhibition were physically separable, with T6P inhibition of SnRK1 dependent on an intermediary factor. In subsequent analysis, T6P inhibited SnRK1 in extracts of all tissues analyzed except those of mature leaves, which did not contain the intermediary factor. To assess the impact of T6P inhibition of SnRK1 in vivo, gene expression was determined in seedlings expressing Escherichia coli otsA encoding T6P synthase to elevate T6P or otsB encoding T6P phosphatase to decrease T6P. SnRK1 target genes showed opposite regulation, consistent with the regulation of SnRK1 by T6P in vivo. Analysis of microarray data showed up-regulation by T6P of genes involved in biosynthetic reactions, such as genes for amino acid, protein, and nucleotide synthesis, the tricarboxylic acid cycle, and mitochondrial electron transport, which are normally down-regulated by SnRK1. In contrast, genes involved in photosynthesis and degradation processes, which are normally up-regulated by SnRK1, were down-regulated by T6P. These experiments provide strong evidence that T6P inhibits SnRK1 to activate biosynthetic processes in growing tissues.</jats:p> Inhibition of SNF1-Related Protein Kinase1 Activity and Regulation of Metabolic Pathways by Trehalose-6-Phosphate Plant Physiology |
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10.1104/pp.108.133934 |
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| title |
Inhibition of SNF1-Related Protein Kinase1 Activity and Regulation of Metabolic Pathways by Trehalose-6-Phosphate |
| title_unstemmed |
Inhibition of SNF1-Related Protein Kinase1 Activity and Regulation of Metabolic Pathways by Trehalose-6-Phosphate |
| title_full |
Inhibition of SNF1-Related Protein Kinase1 Activity and Regulation of Metabolic Pathways by Trehalose-6-Phosphate |
| title_fullStr |
Inhibition of SNF1-Related Protein Kinase1 Activity and Regulation of Metabolic Pathways by Trehalose-6-Phosphate |
| title_full_unstemmed |
Inhibition of SNF1-Related Protein Kinase1 Activity and Regulation of Metabolic Pathways by Trehalose-6-Phosphate |
| title_short |
Inhibition of SNF1-Related Protein Kinase1 Activity and Regulation of Metabolic Pathways by Trehalose-6-Phosphate |
| title_sort |
inhibition of snf1-related protein kinase1 activity and regulation of metabolic pathways by trehalose-6-phosphate |
| topic |
Plant Science Genetics Physiology |
| url |
http://dx.doi.org/10.1104/pp.108.133934 |
| publishDate |
2009 |
| physical |
1860-1871 |
| description |
<jats:title>Abstract</jats:title>
<jats:p>Trehalose-6-phosphate (T6P) is a proposed signaling molecule in plants, yet how it signals was not clear. Here, we provide evidence that T6P functions as an inhibitor of SNF1-related protein kinase1 (SnRK1; AKIN10/AKIN11) of the SNF1-related group of protein kinases. T6P, but not other sugars and sugar phosphates, inhibited SnRK1 in Arabidopsis (Arabidopsis thaliana) seedling extracts strongly (50%) at low concentrations (1–20 μ m). Inhibition was noncompetitive with respect to ATP. In immunoprecipitation studies using antibodies to AKIN10 and AKIN11, SnRK1 catalytic activity and T6P inhibition were physically separable, with T6P inhibition of SnRK1 dependent on an intermediary factor. In subsequent analysis, T6P inhibited SnRK1 in extracts of all tissues analyzed except those of mature leaves, which did not contain the intermediary factor. To assess the impact of T6P inhibition of SnRK1 in vivo, gene expression was determined in seedlings expressing Escherichia coli otsA encoding T6P synthase to elevate T6P or otsB encoding T6P phosphatase to decrease T6P. SnRK1 target genes showed opposite regulation, consistent with the regulation of SnRK1 by T6P in vivo. Analysis of microarray data showed up-regulation by T6P of genes involved in biosynthetic reactions, such as genes for amino acid, protein, and nucleotide synthesis, the tricarboxylic acid cycle, and mitochondrial electron transport, which are normally down-regulated by SnRK1. In contrast, genes involved in photosynthesis and degradation processes, which are normally up-regulated by SnRK1, were down-regulated by T6P. These experiments provide strong evidence that T6P inhibits SnRK1 to activate biosynthetic processes in growing tissues.</jats:p> |
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| author | Zhang, Yuhua, Primavesi, Lucia F., Jhurreea, Deveraj, Andralojc, P. John, Mitchell, Rowan A.C., Powers, Stephen J., Schluepmann, Henriette, Delatte, Thierry, Wingler, Astrid, Paul, Matthew J. |
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| description | <jats:title>Abstract</jats:title> <jats:p>Trehalose-6-phosphate (T6P) is a proposed signaling molecule in plants, yet how it signals was not clear. Here, we provide evidence that T6P functions as an inhibitor of SNF1-related protein kinase1 (SnRK1; AKIN10/AKIN11) of the SNF1-related group of protein kinases. T6P, but not other sugars and sugar phosphates, inhibited SnRK1 in Arabidopsis (Arabidopsis thaliana) seedling extracts strongly (50%) at low concentrations (1–20 μ m). Inhibition was noncompetitive with respect to ATP. In immunoprecipitation studies using antibodies to AKIN10 and AKIN11, SnRK1 catalytic activity and T6P inhibition were physically separable, with T6P inhibition of SnRK1 dependent on an intermediary factor. In subsequent analysis, T6P inhibited SnRK1 in extracts of all tissues analyzed except those of mature leaves, which did not contain the intermediary factor. To assess the impact of T6P inhibition of SnRK1 in vivo, gene expression was determined in seedlings expressing Escherichia coli otsA encoding T6P synthase to elevate T6P or otsB encoding T6P phosphatase to decrease T6P. SnRK1 target genes showed opposite regulation, consistent with the regulation of SnRK1 by T6P in vivo. Analysis of microarray data showed up-regulation by T6P of genes involved in biosynthetic reactions, such as genes for amino acid, protein, and nucleotide synthesis, the tricarboxylic acid cycle, and mitochondrial electron transport, which are normally down-regulated by SnRK1. In contrast, genes involved in photosynthesis and degradation processes, which are normally up-regulated by SnRK1, were down-regulated by T6P. These experiments provide strong evidence that T6P inhibits SnRK1 to activate biosynthetic processes in growing tissues.</jats:p> |
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| institution | DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161 |
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| spelling | Zhang, Yuhua Primavesi, Lucia F. Jhurreea, Deveraj Andralojc, P. John Mitchell, Rowan A.C. Powers, Stephen J. Schluepmann, Henriette Delatte, Thierry Wingler, Astrid Paul, Matthew J. 1532-2548 Oxford University Press (OUP) Plant Science Genetics Physiology http://dx.doi.org/10.1104/pp.108.133934 <jats:title>Abstract</jats:title> <jats:p>Trehalose-6-phosphate (T6P) is a proposed signaling molecule in plants, yet how it signals was not clear. Here, we provide evidence that T6P functions as an inhibitor of SNF1-related protein kinase1 (SnRK1; AKIN10/AKIN11) of the SNF1-related group of protein kinases. T6P, but not other sugars and sugar phosphates, inhibited SnRK1 in Arabidopsis (Arabidopsis thaliana) seedling extracts strongly (50%) at low concentrations (1–20 μ m). Inhibition was noncompetitive with respect to ATP. In immunoprecipitation studies using antibodies to AKIN10 and AKIN11, SnRK1 catalytic activity and T6P inhibition were physically separable, with T6P inhibition of SnRK1 dependent on an intermediary factor. In subsequent analysis, T6P inhibited SnRK1 in extracts of all tissues analyzed except those of mature leaves, which did not contain the intermediary factor. To assess the impact of T6P inhibition of SnRK1 in vivo, gene expression was determined in seedlings expressing Escherichia coli otsA encoding T6P synthase to elevate T6P or otsB encoding T6P phosphatase to decrease T6P. SnRK1 target genes showed opposite regulation, consistent with the regulation of SnRK1 by T6P in vivo. Analysis of microarray data showed up-regulation by T6P of genes involved in biosynthetic reactions, such as genes for amino acid, protein, and nucleotide synthesis, the tricarboxylic acid cycle, and mitochondrial electron transport, which are normally down-regulated by SnRK1. In contrast, genes involved in photosynthesis and degradation processes, which are normally up-regulated by SnRK1, were down-regulated by T6P. These experiments provide strong evidence that T6P inhibits SnRK1 to activate biosynthetic processes in growing tissues.</jats:p> Inhibition of SNF1-Related Protein Kinase1 Activity and Regulation of Metabolic Pathways by Trehalose-6-Phosphate Plant Physiology |
| spellingShingle | Zhang, Yuhua, Primavesi, Lucia F., Jhurreea, Deveraj, Andralojc, P. John, Mitchell, Rowan A.C., Powers, Stephen J., Schluepmann, Henriette, Delatte, Thierry, Wingler, Astrid, Paul, Matthew J., Plant Physiology, Inhibition of SNF1-Related Protein Kinase1 Activity and Regulation of Metabolic Pathways by Trehalose-6-Phosphate, Plant Science, Genetics, Physiology |
| title | Inhibition of SNF1-Related Protein Kinase1 Activity and Regulation of Metabolic Pathways by Trehalose-6-Phosphate |
| title_full | Inhibition of SNF1-Related Protein Kinase1 Activity and Regulation of Metabolic Pathways by Trehalose-6-Phosphate |
| title_fullStr | Inhibition of SNF1-Related Protein Kinase1 Activity and Regulation of Metabolic Pathways by Trehalose-6-Phosphate |
| title_full_unstemmed | Inhibition of SNF1-Related Protein Kinase1 Activity and Regulation of Metabolic Pathways by Trehalose-6-Phosphate |
| title_short | Inhibition of SNF1-Related Protein Kinase1 Activity and Regulation of Metabolic Pathways by Trehalose-6-Phosphate |
| title_sort | inhibition of snf1-related protein kinase1 activity and regulation of metabolic pathways by trehalose-6-phosphate |
| title_unstemmed | Inhibition of SNF1-Related Protein Kinase1 Activity and Regulation of Metabolic Pathways by Trehalose-6-Phosphate |
| topic | Plant Science, Genetics, Physiology |
| url | http://dx.doi.org/10.1104/pp.108.133934 |