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XB-ART-20915
Biochem J 1994 Aug 15;302 ( Pt 1):237-44.
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Structure and expression of the Drosophila ubiquitin-80-amino-acid fusion-protein gene.

Barrio R , del Arco A , Cabrera HL , Arribas C .


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In the fruitfly Drosophila, as in all eukaryotes examined so far, some ubiquitin-coding sequences appear fused to unrelated open reading frames. Two of these fusion genes have been previously described (the homologues of UBI1-UBI2 and UBI4 in yeast), and we report here the organization and expression of a third one, the DUb80 gene (the homologue of UBI3 in yeast). This gene encodes a ubiquitin monomer fused to an 80-amino-acid extension which is homologous with the ribosomal protein encoded by the UB13 gene. The 5' regulatory region of DUb80 shares common features with another ubiquitin fusion gene, DUb52, and with the ribosomal protein genes of Drosophila, Xenopus and mouse. We also find helix-loop-helix protein-binding sequences (E-boxes). The DUb80 gene is transcribed to a 0.9 kb mRNA which is particularly abundant under conditions of high protein synthesis, such as in ovaries and exponentially growing cells.

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References [+] :
Anthony-Cahill, Molecular characterization of helix-loop-helix peptides. 1992, Pubmed