Characterization and function of an E2-17 kDa (UBE2D) in an invertebrate Haliotis diversicolor supertexta |
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Authors: | Shigen Ye Liuji Wu Ming Luo Ting Xu Xinzhong Wu |
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Affiliation: | 1. Laboratory of Marine Life Science and Technology, College of Animal Sciences, Zhejiang University, 268 Kaixuan Road, Hangzhou, Zhejiang 310029, PR China;2. College of Fisheries and Life Science, Dalian Ocean University, 52 Heishijiao Road, Dalian 116023, PR China;3. College of Agronomy, Henan Agricultural University, 63 Nongye Road, Zhengzhou 450002, PR China;4. Hainan Provincial Fisheries Research Institute, 54 Haifu Road, Haikou 570203, PR China |
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Abstract: | Ubiquitin-conjugating enzymes (UBE2s or E2s) are characterized by the presence of a highly conserved ubiquitin-conjugating (UBC) domain, which predominantly determines the type of ubiquitin chains and directly controls the cellular fate of the substrate. In this study, an E2 homolog was identified and functionally characterized in abalone, which we named ab-UBE2D. The full-length cDNA consists of 1005 bp with an ORF encoding a protein of 147 amino acids. The deduced amino acid sequence shows ab-UBE2D shares conserved UBC domain with other E2 proteins and belongs to class I E2 enzyme family, which are further confirmed by phylogenetic tree analysis. Real-time PCR and western blot analyses showed that ab-UBE2D was ubiquitously expressed in abalone and the expression level of ab-UBE2d was significantly induced by LPS and Poly (I:C). Immunofluorescence microscopy staining demonstrated that native ab-UBE2D was mainly distributed in the cytoplast. Ubiquitination assay showed that ab-UBE2D had ubiquitin conjugating activity to form the enzyme-(Ub)n conjugates. Taken together, these results strongly suggest that ab-UBE2D is an E2 homolog and it may be involved in the immune response of abalone, Haliotis diversicolor supertexta. |
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Keywords: | UBE2D Ubiquitin-conjugating activity Immune response |
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