Diversification of SUMO-activating enzyme in Arabidopsis: Implications in SUMO conjugatio
| Autor: | Laura Castaño-Miquel, Silvia Manrique, Félix A. Atencio, Josep Seguí, Inês Teixeira, L. Maria Lois, Lorenzo Carretero-Paulet |
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| Přispěvatelé: | European Commission, European Research Council, Ministerio de Educación y Ciencia (España), Generalitat de Catalunya |
| Rok vydání: | 2013 |
| Předmět: |
0106 biological sciences
Gene isoform Protein subunit Molecular Sequence Data Mutant Arabidopsis SUMO protein SUMO enzymes Ubiquitin-Activating Enzymes Plant Science Genes Plant 01 natural sciences Evolution Molecular 03 medical and health sciences Stress Physiological Protein Isoforms Amino Acid Sequence Molecular Biology Gene Conserved Sequence Phylogeny 030304 developmental biology 0303 health sciences biology Arabidopsis Proteins Sumoylation Bayes Theorem biology.organism_classification Kinetics Biochemistry Mutation Small Ubiquitin-Related Modifier Proteins Nuclear localization sequence Subcellular Fractions 010606 plant biology & botany |
| Zdroj: | Digital.CSIC: Repositorio Institucional del CSIC Consejo Superior de Investigaciones Científicas (CSIC) Digital.CSIC. Repositorio Institucional del CSIC instname Molecular Plant |
| DOI: | 10.13039/501100000781 |
| Popis: | Sumoylation is an essential posttranslational modification that participates in many biological processes including stress responses. However, little is known about the mechanisms that control Small Ubiquitin-like MOdifier (SUMO) conjugation in vivo. We have evaluated the regulatory role of the heterodimeric E1 activating enzyme, which catalyzes the first step in SUMO conjugation. We have established that the E1 large SAE2 and small SAE1 subunits are encoded by one and three genes, respectively, in the Arabidopsis genome. The three paralogs genes SAE1a, SAE1b1, and SAE1b2 are the result of two independent duplication events. Since SAE1b1 and SAE1b2 correspond to two identical copies, only two E1 small subunit isoforms are present in vivo: SAE1a and SAE1b. The E1 heterodimer nuclear localization is modulated by the C-terminal tail of the SAE2 subunit. In vitro, SUMO conjugation rate is dependent on the SAE1 isoform contained in the E1 holoenzyme and our results suggest that downstream steps to SUMO–E1 thioester bond formation are affected. In vivo, SAE1a isoform deletion in T-DNA insertion mutant plants conferred sumoylation defects upon abiotic stress, consistent with a sumoylation defective phenotype. Our results support previous data pointing to a regulatory role of the E1 activating enzyme during SUMO conjugation and provide a novel mechanism to control sumoylation in vivo by diversification of the E1 small subunit. This work was supported by the European Research Council (grant ERC-2007-StG-205927) and the Spanish Ministry of Education and Science (grant BIO2008-01495 and CONSOLIDER CSD 2007–00036). L.C.M., S.M., I.T., and F.A. were supported by research contracts trough the CRAG. J.S. was supported by a pre-doctoral fellowship from the Ministry of Education and Science (BES-2005–6843). We also thank the Departament d’Innovació, Universitats i Empresa from the Generalitat de Catalunya (Xarxa de Referència en Biotecnologia and 2009SGR 09626) for substantial support. |
| Databáze: | OpenAIRE |
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