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Deficient glutamate biosynthesis triggers a concerted upregulation of ribosomal protein genes in Arabidopsis

Biomass production requires the coordination between growth and metabolism. In a large-scale screen for mutants affected in leaf morphology, we isolated the orbiculata1 (orb1) mutants, which exhibit a pale green phenotype and reduced growth. The combination of map-based cloning and next-generation s...

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Autores principales: Muñoz-Nortes, Tamara, Pérez-Pérez, José Manuel, Sarmiento-Mañús, Raquel, Candela, Héctor, Micol, José Luis
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5522406/
https://www.ncbi.nlm.nih.gov/pubmed/28733652
http://dx.doi.org/10.1038/s41598-017-06335-4
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author Muñoz-Nortes, Tamara
Pérez-Pérez, José Manuel
Sarmiento-Mañús, Raquel
Candela, Héctor
Micol, José Luis
author_facet Muñoz-Nortes, Tamara
Pérez-Pérez, José Manuel
Sarmiento-Mañús, Raquel
Candela, Héctor
Micol, José Luis
author_sort Muñoz-Nortes, Tamara
collection PubMed
description Biomass production requires the coordination between growth and metabolism. In a large-scale screen for mutants affected in leaf morphology, we isolated the orbiculata1 (orb1) mutants, which exhibit a pale green phenotype and reduced growth. The combination of map-based cloning and next-generation sequencing allowed us to establish that ORB1 encodes the GLUTAMATE SYNTHASE 1 (GLU1) enzyme, also known as FERREDOXIN-DEPENDENT GLUTAMINE OXOGLUTARATE AMINOTRANSFERASE 1 (Fd-GOGAT1). We performed an RNA-seq analysis to identify global gene expression changes in the orb1–3 mutant. We found altered expression levels of genes encoding enzymes involved in nitrogen assimilation and amino acid biosynthesis, such as glutamine synthetases, asparagine synthetases and glutamate dehydrogenases, showing that the expression of these genes depends on the levels of glutamine and/or glutamate. In addition, we observed a concerted upregulation of genes encoding subunits of the cytosolic ribosome. A gene ontology (GO) analysis of the differentially expressed genes between Ler and orb1–3 showed that the most enriched GO terms were ‘translation’, ‘cytosolic ribosome’ and ‘structural constituent of ribosome’. The upregulation of ribosome-related functions might reflect an attempt to keep protein synthesis at optimal levels even when the pool of glutamate is reduced.
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spelling pubmed-55224062017-07-26 Deficient glutamate biosynthesis triggers a concerted upregulation of ribosomal protein genes in Arabidopsis Muñoz-Nortes, Tamara Pérez-Pérez, José Manuel Sarmiento-Mañús, Raquel Candela, Héctor Micol, José Luis Sci Rep Article Biomass production requires the coordination between growth and metabolism. In a large-scale screen for mutants affected in leaf morphology, we isolated the orbiculata1 (orb1) mutants, which exhibit a pale green phenotype and reduced growth. The combination of map-based cloning and next-generation sequencing allowed us to establish that ORB1 encodes the GLUTAMATE SYNTHASE 1 (GLU1) enzyme, also known as FERREDOXIN-DEPENDENT GLUTAMINE OXOGLUTARATE AMINOTRANSFERASE 1 (Fd-GOGAT1). We performed an RNA-seq analysis to identify global gene expression changes in the orb1–3 mutant. We found altered expression levels of genes encoding enzymes involved in nitrogen assimilation and amino acid biosynthesis, such as glutamine synthetases, asparagine synthetases and glutamate dehydrogenases, showing that the expression of these genes depends on the levels of glutamine and/or glutamate. In addition, we observed a concerted upregulation of genes encoding subunits of the cytosolic ribosome. A gene ontology (GO) analysis of the differentially expressed genes between Ler and orb1–3 showed that the most enriched GO terms were ‘translation’, ‘cytosolic ribosome’ and ‘structural constituent of ribosome’. The upregulation of ribosome-related functions might reflect an attempt to keep protein synthesis at optimal levels even when the pool of glutamate is reduced. Nature Publishing Group UK 2017-07-21 /pmc/articles/PMC5522406/ /pubmed/28733652 http://dx.doi.org/10.1038/s41598-017-06335-4 Text en © The Author(s) 2017 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/.
spellingShingle Article
Muñoz-Nortes, Tamara
Pérez-Pérez, José Manuel
Sarmiento-Mañús, Raquel
Candela, Héctor
Micol, José Luis
Deficient glutamate biosynthesis triggers a concerted upregulation of ribosomal protein genes in Arabidopsis
title Deficient glutamate biosynthesis triggers a concerted upregulation of ribosomal protein genes in Arabidopsis
title_full Deficient glutamate biosynthesis triggers a concerted upregulation of ribosomal protein genes in Arabidopsis
title_fullStr Deficient glutamate biosynthesis triggers a concerted upregulation of ribosomal protein genes in Arabidopsis
title_full_unstemmed Deficient glutamate biosynthesis triggers a concerted upregulation of ribosomal protein genes in Arabidopsis
title_short Deficient glutamate biosynthesis triggers a concerted upregulation of ribosomal protein genes in Arabidopsis
title_sort deficient glutamate biosynthesis triggers a concerted upregulation of ribosomal protein genes in arabidopsis
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5522406/
https://www.ncbi.nlm.nih.gov/pubmed/28733652
http://dx.doi.org/10.1038/s41598-017-06335-4
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