In the fruitfly Drosophila, as in all eukaryotes examined so far, some
ubiquitin-coding sequences appear fused to unrelated open reading fra
mes. Two of these fusion genes have been previously described (the hom
ologues of UBI1-UBI2 and UBI4 in yeast), and we report here the organi
zation 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 en
coded by the UBI3 gene. The 5' regulatory region of DUb80 shares commo
n features with another ubiquitin fusion gene, DUb52, and with the rib
osomal protein genes of Drosophila, Xenopus and mouse. We also find he
lix-loop-helix protein-binding sequences (E-boxes). The DUb80 gene is
transcribed to a 0.9 kb mRNA which is particularly abundant under cond
itions of high protein synthesis, such as in ovaries and exponentially
growing cells.