Artículos de revistas
Characterization of the Arabidopsis thaliana E3 Ubiquitin-Ligase AtSINAL7 and identification of the Ubiquitination sites
Fecha
2013-08Registro en:
Peralta, Diego Alberto; Araya, Alejandro; Nardi, Cristina Fernanda; Busi, María Victoria; Gomez Casati, Diego Fabian; Characterization of the Arabidopsis thaliana E3 Ubiquitin-Ligase AtSINAL7 and identification of the Ubiquitination sites; Public Library Science; Plos One; 8; 8; 8-2013; 1-10; e731
1932-6203
CONICET Digital
CONICET
Autor
Peralta, Diego Alberto
Araya, Alejandro
Nardi, Cristina Fernanda
Busi, María Victoria
Gomez Casati, Diego Fabian
Resumen
Protein ubiquitination leading to degradation by the proteasome is an important mechanism in regulating key cellular functions. Protein ubiquitination is carried out by a three step process involving ubiquitin (Ub) activation by a E1 enzyme, the transfer of Ub to a protein E2, finally an ubiquitin ligase E3 catalyzes the transfer of the Ub peptide to an acceptor protein. The E3 component is responsible for the specific recognition of the target, making the unveiling of E3 components essential to understand the mechanisms regulating fundamental cell processes through the protein degradation pathways. The Arabidopsis thaliana seven in absentia-like 7 (AtSINAL7) gene encodes for a protein with characteristics from a C3HC4-type E3 ubiquitin ligase. We demonstrate here that AtSINAL7 protein is indeed an E3 protein ligase based on the self-ubiquitination in vitro assay. This activity is dependent of the presence of a Lys residue in position 124. We also found that higher AtSINAL7 transcript levels are present in tissues undergoing active cell division during floral development. An interesting observation is the circadian expression pattern of AtSINAL7 mRNA in floral buds. Furthermore, UV–B irradiation induces the expression of this transcript indicating that AtSINAL7 may be involved in a wide range of different cell processes.