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Glutamine synthetase in Medicago truncatula, unveiling new secrets of a very old enzyme
Glutamine synthetase (GS) catalyzes the first step at which nitrogen is brought into cellular metabolism and is also involved in the reassimilation of ammonium released by a number of metabolic pathways. Due to its unique position in plant nitrogen metabolism, GS plays essential roles in all aspects...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2015
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4515544/ https://www.ncbi.nlm.nih.gov/pubmed/26284094 http://dx.doi.org/10.3389/fpls.2015.00578 |
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author | Seabra, Ana R. Carvalho, Helena G. |
author_facet | Seabra, Ana R. Carvalho, Helena G. |
author_sort | Seabra, Ana R. |
collection | PubMed |
description | Glutamine synthetase (GS) catalyzes the first step at which nitrogen is brought into cellular metabolism and is also involved in the reassimilation of ammonium released by a number of metabolic pathways. Due to its unique position in plant nitrogen metabolism, GS plays essential roles in all aspects of plant development, from germination to senescence, and is a key component of nitrogen use efficiency (NUE) and plant yield. Understanding the mechanisms regulating GS activity is therefore of utmost importance and a great effort has been dedicated to understand how GS is regulated in different plant species. The present review summarizes exciting recent developments concerning the structure and regulation of GS isoenzymes, using the model legume Medicago truncatula. These include the understanding of the structural determinants of both the cytosolic and plastid located isoenzymes, the existence of a seed-specific GS gene unique to M. truncatula and closely related species and the discovery that GS isoenzymes are regulated by nitric oxide at the post-translational level. The data is discussed and integrated with the potential roles of the distinct GS isoenzymes within the whole plant context. |
format | Online Article Text |
id | pubmed-4515544 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-45155442015-08-17 Glutamine synthetase in Medicago truncatula, unveiling new secrets of a very old enzyme Seabra, Ana R. Carvalho, Helena G. Front Plant Sci Plant Science Glutamine synthetase (GS) catalyzes the first step at which nitrogen is brought into cellular metabolism and is also involved in the reassimilation of ammonium released by a number of metabolic pathways. Due to its unique position in plant nitrogen metabolism, GS plays essential roles in all aspects of plant development, from germination to senescence, and is a key component of nitrogen use efficiency (NUE) and plant yield. Understanding the mechanisms regulating GS activity is therefore of utmost importance and a great effort has been dedicated to understand how GS is regulated in different plant species. The present review summarizes exciting recent developments concerning the structure and regulation of GS isoenzymes, using the model legume Medicago truncatula. These include the understanding of the structural determinants of both the cytosolic and plastid located isoenzymes, the existence of a seed-specific GS gene unique to M. truncatula and closely related species and the discovery that GS isoenzymes are regulated by nitric oxide at the post-translational level. The data is discussed and integrated with the potential roles of the distinct GS isoenzymes within the whole plant context. Frontiers Media S.A. 2015-07-27 /pmc/articles/PMC4515544/ /pubmed/26284094 http://dx.doi.org/10.3389/fpls.2015.00578 Text en Copyright © 2015 Seabra and Carvalho. 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) or licensor 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 Seabra, Ana R. Carvalho, Helena G. Glutamine synthetase in Medicago truncatula, unveiling new secrets of a very old enzyme |
title | Glutamine synthetase in Medicago truncatula, unveiling new secrets of a very old enzyme |
title_full | Glutamine synthetase in Medicago truncatula, unveiling new secrets of a very old enzyme |
title_fullStr | Glutamine synthetase in Medicago truncatula, unveiling new secrets of a very old enzyme |
title_full_unstemmed | Glutamine synthetase in Medicago truncatula, unveiling new secrets of a very old enzyme |
title_short | Glutamine synthetase in Medicago truncatula, unveiling new secrets of a very old enzyme |
title_sort | glutamine synthetase in medicago truncatula, unveiling new secrets of a very old enzyme |
topic | Plant Science |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4515544/ https://www.ncbi.nlm.nih.gov/pubmed/26284094 http://dx.doi.org/10.3389/fpls.2015.00578 |
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