ArticleJournal of experimental botany2015
New isoforms and assembly of glutamine synthetase in the leaf of wheat (Triticum aestivum L.).
Article in Journal of experimental botany, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 28 citations in OpenAlex.
- Glutamine Synthetase and Glutamate Synthase Family Perform Diverse Physiological Functions in Exogenous Hormones and Abiotic Stress Responses inPlants (Basel, Switzerland) · 2024Article
- The Role of Glutamine Synthetase (GS) and Glutamate Synthase (GOGAT) in the Improvement of Nitrogen Use Efficiency in Cereals.Biomolecules · 2023Review
- Proteomic Analysis ofPlants (Basel, Switzerland) · 2023Article
- Development and marker-trait relationships of functional markers for glutamine synthetaseMolecular breeding : new strategies in plant improvement · 2023Article
- Proteomic responses of two spring wheat cultivars to the combined water deficit and aphid (Frontiers in plant science · 2022Article
- A New Perspective on the Role of Glutamine Synthetase in Nitrogen Remobilization in Wheat (International journal of molecular sciences · 2021Article
- Multimerization variants as potential drivers of neofunctionalization.Science advances · 2021Article
- Localization, Gene Expression, and Functions of Glutamine Synthetase Isozymes in Wheat Grain (Frontiers in plant science · 2021Article
- Nitrogen Regulating the Expression and Localization of Four Glutamine Synthetase Isoforms in Wheat (International journal of molecular sciences · 2020Article
- Cytosolic GLUTAMINE SYNTHETASE1;1 Modulates Metabolism and Chloroplast Development in Roots.Plant physiology · 2020Article
- Cisgenic overexpression of cytosolic glutamine synthetase improves nitrogen utilization efficiency in barley and prevents grain protein decline under elevated COPlant biotechnology journal · 2019Article
- Comparative Proteomic Analysis Unveils Critical Pathways Underlying the Role of Nitrogen Fertilizer Treatment in American Elderberry.Proteomes · 2019Article
- Chloroplast Glutamine Synthetase, the Key Regulator of Nitrogen Metabolism in Wheat, Performs Its Role by Fine Regulation of Enzyme Activity via Negative Cooperativity of Its Subunits.Frontiers in plant science · 2018Article
- The Effect of PoplarFrontiers in plant science · 2018Article
- The role of glutamine synthetase isozymes in enhancing nitrogen use efficiency of N-efficient winter wheat.Scientific reports · 2017Article
- Influence of different host associations on glutamine synthetase activity and ammonium transporter inPhysiology and molecular biology of plants : an international journal of functional plant biology · 2016Article
- Cytosolic Glutamine Synthetase Gln1;2 Is the Main Isozyme Contributing to GS1 Activity and Can Be Up-Regulated to Relieve Ammonium Toxicity.Plant physiology · 2016Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glutamine synthetase (GS; EC 6.3.1.2) plays a crucial role in the assimilation and re-assimilation of ammonia derived from a wide variety of metabolic processes during plant growth and development. Here, three developmentally regulated isoforms of GS holoenzyme in the leaf of wheat (Triticum aestivum L.) seedlings are described using native-PAGE with a transferase activity assay. The isoforms showed different mobilities in gels, with GSII>GSIII>GSI. The cytosolic GSI was composed of three subunits, GS1, GSr1, and GSr2, with the same molecular weight (39.2kDa), but different pI values. GSI appeared at leaf emergence and was active throughout the leaf lifespan. GSII and GSIII, both located in the chloroplast, were each composed of a single 42.1kDa subunit with different pI values. GSII was active mainly in green leaves, while GSIII showed brief but higher activity in green leaves grown under field conditions. LC-MS/MS experiments revealed that GSII and GSIII have the same amino acid sequence, but GSII has more modification sites. With a modified blue native electrophoresis (BNE) technique and in-gel catalytic activity analysis, only two GS isoforms were observed: one cytosolic and one chloroplastic. Mass calibrations on BNE gels showed that the cytosolic GS1 holoenzyme was ~490kDa and likely a dodecamer, and the chloroplastic GS2 holoenzyme was ~240kDa and likely a hexamer. Our experimental data suggest that the activity of GS isoforms in wheat is regulated by subcellular localization, assembly, and modification to achieve their roles during plant development.
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