Cloning of a novel ubiquitin-conjugating enzyme (E2) gene from the ciliate Paramecium tetraurelia.
We isolated a 1.7 kb gene (UbcP1) for a ubiquitin-conjugating enzyme from a P. tetraurelia cDNA library and sequenced it. Its deduced polypeptide sequence consists of 425 amino acid residues (48 kDa). The UbcP1 protein contains novel N- and C-terminal extensions in addition to a UBC domain, and within the UBC domain it shares low identity with sequences of other known E2s. A constructed phylogenetic tree suggests that the UbcP1 protein may represent a member of a distinct subfamily of E2s. Southern blot analysis showed that the N-terminal extension of the UbcP1 is conserved in P. multimicronucleatum.
Okano
S
S
Department of Biophysical Engineering, Faculty of Engineering Science, Osaka University, Japan.
Tokushima
H
H
Nakaoka
Y
Y
Shimizu
K
K
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015139:Blotting, Southern; D003001:Cloning, Molecular; D017124:Conserved Sequence; D017931:DNA Primers; D015342:DNA Probes; D018076:DNA, Complementary; D016054:DNA, Protozoan / Q000032:analysis; D015723:Gene Library; D017125:Genes, Protozoan; D006801:Humans; D008025:Ligases / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics; D008969:Molecular Sequence Data; D016805:Paramecium tetraurelia / Q000201:enzymology* / Q000235:genetics*; D010802:Phylogeny; D016133:Polymerase Chain Reaction; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry; D017386:Sequence Homology, Amino Acid; D044763:Ubiquitin-Conjugating Enzymes
D017931:DNA Primers; D015342:DNA Probes; D018076:DNA, Complementary; D016054:DNA, Protozoan; D011994:Recombinant Proteins; D044763:Ubiquitin-Conjugating Enzymes; D008025:Ligases