Novel Glutamate–Putrescine Ligase Activity in <i>Haloferax mediterranei</i>: A New Function for <i>glnA-2</i> Gene
The genome of the halophilic archaea <i>Haloferax mediterranei</i> contains three ORFs that show homology with glutamine synthetase (GS) (<i>glnA-1</i>, <i>glnA-2</i>, and <i>glnA-3</i>). Previous studies have focused on the role of GlnA-1, suggesting...
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MDPI AG
2021-08-01
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| Series: | Biomolecules |
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| Online Access: | https://www.mdpi.com/2218-273X/11/8/1156 |
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| author | Verónica Rodríguez-Herrero Arnau Peris Mónica Camacho Vanesa Bautista Julia Esclapez María-José Bonete |
| author_facet | Verónica Rodríguez-Herrero Arnau Peris Mónica Camacho Vanesa Bautista Julia Esclapez María-José Bonete |
| author_sort | Verónica Rodríguez-Herrero |
| collection | DOAJ |
| description | The genome of the halophilic archaea <i>Haloferax mediterranei</i> contains three ORFs that show homology with glutamine synthetase (GS) (<i>glnA-1</i>, <i>glnA-2</i>, and <i>glnA-3</i>). Previous studies have focused on the role of GlnA-1, suggesting that proteins GlnA-2 and GlnA-3 could play a different role to that of GS. Glutamine synthetase (EC 6.3.1.2) belongs to the class of ligases, including 20 subclasses of other different enzymes, such as aspartate–ammonia ligase (EC 6.3.1.1), glutamate–ethylamine ligase (EC 6.3.1.6), and glutamate–putrescine ligase (EC 6.3.1.11). The reaction catalyzed by glutamate–putrescine ligase is comparable to the reaction catalyzed by glutamine synthetase (GS). Both enzymes can bind a glutamate molecule to an amino group: ammonium (GS) or putrescine (glutamate–putrescine ligase). In addition, they present the characteristic catalytic domain of GS, showing significant similarities in their structure. Although these proteins are annotated as GS, the bioinformatics and experimental results obtained in this work indicate that the GlnA-2 protein (HFX_1688) is a glutamate–putrescine ligase, involved in polyamine catabolism. The most significant results are those related to glutamate–putrescine ligase’s activity and the analysis of the transcriptional and translational expression of the <i>glnA-2</i> gene in the presence of different nitrogen sources. This work confirms a new metabolic pathway in the <i>Archaea</i> domain which extends the knowledge regarding the utilization of alternative nitrogen sources in this domain. |
| first_indexed | 2024-03-10T08:58:40Z |
| format | Article |
| id | doaj.art-a8b2caa527684d5f81dcb33c30e8447a |
| institution | Directory Open Access Journal |
| issn | 2218-273X |
| language | English |
| last_indexed | 2024-03-10T08:58:40Z |
| publishDate | 2021-08-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biomolecules |
| spelling | doaj.art-a8b2caa527684d5f81dcb33c30e8447a2023-11-22T06:55:38ZengMDPI AGBiomolecules2218-273X2021-08-01118115610.3390/biom11081156Novel Glutamate–Putrescine Ligase Activity in <i>Haloferax mediterranei</i>: A New Function for <i>glnA-2</i> GeneVerónica Rodríguez-Herrero0Arnau Peris1Mónica Camacho2Vanesa Bautista3Julia Esclapez4María-José Bonete5Agrochemistry and Biochemistry Department, Biochemistry and Molecular Biology Division, Faculty of Science, University of Alicante, 03080 Alicante, SpainInstitute for Integrative Systems Biology, I2SysBio, Campus Burjassot, University of Valencia-CSIC, 46908 Valencia, SpainAgrochemistry and Biochemistry Department, Biochemistry and Molecular Biology Division, Faculty of Science, University of Alicante, 03080 Alicante, SpainAgrochemistry and Biochemistry Department, Biochemistry and Molecular Biology Division, Faculty of Science, University of Alicante, 03080 Alicante, SpainAgrochemistry and Biochemistry Department, Biochemistry and Molecular Biology Division, Faculty of Science, University of Alicante, 03080 Alicante, SpainAgrochemistry and Biochemistry Department, Biochemistry and Molecular Biology Division, Faculty of Science, University of Alicante, 03080 Alicante, SpainThe genome of the halophilic archaea <i>Haloferax mediterranei</i> contains three ORFs that show homology with glutamine synthetase (GS) (<i>glnA-1</i>, <i>glnA-2</i>, and <i>glnA-3</i>). Previous studies have focused on the role of GlnA-1, suggesting that proteins GlnA-2 and GlnA-3 could play a different role to that of GS. Glutamine synthetase (EC 6.3.1.2) belongs to the class of ligases, including 20 subclasses of other different enzymes, such as aspartate–ammonia ligase (EC 6.3.1.1), glutamate–ethylamine ligase (EC 6.3.1.6), and glutamate–putrescine ligase (EC 6.3.1.11). The reaction catalyzed by glutamate–putrescine ligase is comparable to the reaction catalyzed by glutamine synthetase (GS). Both enzymes can bind a glutamate molecule to an amino group: ammonium (GS) or putrescine (glutamate–putrescine ligase). In addition, they present the characteristic catalytic domain of GS, showing significant similarities in their structure. Although these proteins are annotated as GS, the bioinformatics and experimental results obtained in this work indicate that the GlnA-2 protein (HFX_1688) is a glutamate–putrescine ligase, involved in polyamine catabolism. The most significant results are those related to glutamate–putrescine ligase’s activity and the analysis of the transcriptional and translational expression of the <i>glnA-2</i> gene in the presence of different nitrogen sources. This work confirms a new metabolic pathway in the <i>Archaea</i> domain which extends the knowledge regarding the utilization of alternative nitrogen sources in this domain.https://www.mdpi.com/2218-273X/11/8/1156glutamine synthetaseglutamate–putrescine ligasenitrogen assimilationputrescinehaloarchaea |
| spellingShingle | Verónica Rodríguez-Herrero Arnau Peris Mónica Camacho Vanesa Bautista Julia Esclapez María-José Bonete Novel Glutamate–Putrescine Ligase Activity in <i>Haloferax mediterranei</i>: A New Function for <i>glnA-2</i> Gene Biomolecules glutamine synthetase glutamate–putrescine ligase nitrogen assimilation putrescine haloarchaea |
| title | Novel Glutamate–Putrescine Ligase Activity in <i>Haloferax mediterranei</i>: A New Function for <i>glnA-2</i> Gene |
| title_full | Novel Glutamate–Putrescine Ligase Activity in <i>Haloferax mediterranei</i>: A New Function for <i>glnA-2</i> Gene |
| title_fullStr | Novel Glutamate–Putrescine Ligase Activity in <i>Haloferax mediterranei</i>: A New Function for <i>glnA-2</i> Gene |
| title_full_unstemmed | Novel Glutamate–Putrescine Ligase Activity in <i>Haloferax mediterranei</i>: A New Function for <i>glnA-2</i> Gene |
| title_short | Novel Glutamate–Putrescine Ligase Activity in <i>Haloferax mediterranei</i>: A New Function for <i>glnA-2</i> Gene |
| title_sort | novel glutamate putrescine ligase activity in i haloferax mediterranei i a new function for i glna 2 i gene |
| topic | glutamine synthetase glutamate–putrescine ligase nitrogen assimilation putrescine haloarchaea |
| url | https://www.mdpi.com/2218-273X/11/8/1156 |
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