melanogaster SINA regulates photoreceptor differentiation by targeting the transcription factor Tramtrack for proteasomal degradation. First described in Drosophila melanogaster, Seven in absentia (SINA) proteins are E3 ubiquitin ligases with a characteristic N-terminal RING (Really Interesting New Gene) finger domain, linked to a conserved C-terminal domain required for oligomerization and binding to target proteins. Protein turnover through the ubiquitin-mediated proteasome system plays a pivotal role in many regulatory pathways such as growth, cell differentiation, cell cycle control, stress response and apoptosis. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.Ĭompeting interests: The authors have declared that no competing interests exist. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.įunding: This work was supported by grants from ANPCyT (PICT 07), the PICS-CNRS Program 3641 and the Institut National de Recherche Agronimique (INRA, France). Received: JAccepted: JPublished: August 28, 2013Ĭopyright: © 2013 Peralta et al. PLoS ONE 8(8):Įditor: Miguel A Blazquez, Instituto de Biología Molecular y Celular de Plantas, Spain Furthermore, UV–B irradiation induces the expression of this transcript indicating that AtSINAL7 may be involved in a wide range of different cell processes.Ĭitation: Peralta DA, Araya A, Nardi CF, Busi MV, Gomez-Casati DF (2013) Characterization of the Arabidopsis thaliana E3 Ubiquitin-Ligase AtSINAL7 and Identification of the Ubiquitination Sites. An interesting observation is the circadian expression pattern of AtSINAL7 mRNA in floral buds. We also found that higher AtSINAL7 transcript levels are present in tissues undergoing active cell division during floral development. This activity is dependent of the presence of a Lys residue in position 124. We demonstrate here that AtSINAL7 protein is indeed an E3 protein ligase based on the self-ubiquitination in vitro assay. The Arabidopsis thaliana seven in absentia-like 7 ( AtSINAL7) gene encodes for a protein with characteristics from a C3HC4-type E3 ubiquitin ligase. 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. 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. Protein ubiquitination leading to degradation by the proteasome is an important mechanism in regulating key cellular functions.
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