ArticlePlant physiology2003
Expression of the plastid-located glutamine synthetase of Medicago truncatula. Accumulation of the precursor in root nodules reveals an in vivo control at the level of protein import into plastids.
Article in Plant physiology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 53 citations in OpenAlex.
- Article
- Characterization of the Glutamine Synthetase Gene Family in Wheat (International journal of molecular sciences · 2025Article
- Effects of Biological Nitrogen Metabolism on Glufosinate-Susceptible and -Resistant Goosegrass (International journal of molecular sciences · 2023Article
- Signaling by reactive molecules and antioxidants in legume nodules.The New phytologist · 2022Review
- A Natural Light/Dark Cycle Regulation of Carbon-Nitrogen Metabolism and Gene Expression in Rice Shoots.Frontiers in plant science · 2016Article
- Overexpressing of OsAMT1-3, a High Affinity Ammonium Transporter Gene, Modifies Rice Growth and Carbon-Nitrogen Metabolic Status.International journal of molecular sciences · 2015Article
- Glutamine synthetase in Medicago truncatula, unveiling new secrets of a very old enzyme.Frontiers in plant science · 2015Review
- The structures of cytosolic and plastid-located glutamine synthetases from Medicago truncatula reveal a common and dynamic architecture.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Characterization of a glutamine synthetase gene DvGS1 from Dunaliella viridis and investigation of the impact on expression of DvGS1 in transgenic Arabidopsis thaliana.Molecular biology reports · 2014Article
- Article
- Multiple complexes of nitrogen assimilatory enzymes in spinach chloroplasts: possible mechanisms for the regulation of enzyme function.PloS one · 2014Article
- Novel aspects of glutamine synthetase (GS) regulation revealed by a detailed expression analysis of the entire GS gene family of Medicago truncatula under different physiological conditions.BMC plant biology · 2013Article
- Possible role of glutamine synthetase in the NO signaling response in root nodules by contributing to the antioxidant defenses.Frontiers in plant science · 2013Article
- Glutamine synthetase in legumes: recent advances in enzyme structure and functional genomics.International journal of molecular sciences · 2012Review
- Glutamine synthetase is a molecular target of nitric oxide in root nodules of Medicago truncatula and is regulated by tyrosine nitration.Plant physiology · 2011Article
- Medicago truncatula contains a second gene encoding a plastid located glutamine synthetase exclusively expressed in developing seeds.BMC plant biology · 2010Article
- Over-expression of aspartate aminotransferase genes in rice resulted in altered nitrogen metabolism and increased amino acid content in seeds.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2009Article
- Overexpressed glutamine synthetase gene modifies nitrogen metabolism and abiotic stress responses in rice.Plant cell reports · 2009Article
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- Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this paper, we report the cloning and characterization of the plastid-located glutamine synthetase (GS) of Medicago truncatula Gaertn (MtGS2). A cDNA was isolated encoding a GS2 precursor polypeptide of 428 amino acids composing an N-terminal transit peptide of 49 amino acids. Expression analysis, by Westerns and by northern hybridization, revealed that MtGS2 is expressed in both photosynthetic and non-photosynthetic organs. Both transcripts and proteins of MtGS2 were detected in substantial amounts in root nodules, suggesting that the enzyme might be performing some important role in this organ. Surprisingly, about 40% of the plastid GS in nodules occurred in the non-processed precursor form (preGS2). This precursor was not detected in any other organ studied and moreover was not observed in non-fixing nodules. Cellular fractionation of nodule extracts revealed that preGS2 is associated with the plastids and that it is catalytically inactive. Immunogold electron microscopy revealed a frequent coincidence of GS with the plastid envelope. Taken together, these results suggest a nodule-specific accumulation of the GS2 precursor at the surface of the plastids in nitrogen-fixing nodules. These results may reflect a regulation of GS2 activity in relation to nitrogen fixation at the level of protein import into nodule plastids.
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