Abstract
Rbx1 (RING box1) is an evolutionarily conserved RING-H2 finger protein and belongs to the RING-finger family of Ubiquitin ligase E3, which determines the substrate specificity of ubiquitination and regulates a variety of biological processes. We report here the identification and functional characterization of an Rbx1 homologue in abalone, which we named ab-Rbx1. Ab-Rbx1 contains conserved cysteine/histidine residues which are the characteristics of Rbx proteins. Phylogenetic tree analysis further demonstrated that ab-Rbx1 belongs to the Rbx1 family other than Rbx2 family. Real-time PCR analysis revealed that ab-Rbx1 was ubiquitously expressed in all examined tissues of abalone and the expression level of ab-Rbx1 was significantly induced by mitogenic situation. Immunohistochemical and immunofluorescent staining showed that the ab-Rbx1 was expressed predominantly in epithelial cells and localized both in the cytoplasmic and nuclear compartment. Ubiquitination assay demonstrated that ab-Rbx1 had ubiquitin ligase activity and could auto-ubiquitinated itself. These results suggest that ab-Rbx1 is an Rbx1 homologue and may be indirectly involved in the immune response of abalone through ubiquitination.
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