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Cloning of a novel ubiquitin‐conjugating enzyme (E2) gene from the ciliate Paramecium tetraurelia
Author(s) -
Okano Satoshi,
Tokushima Hideyuki,
Nakaoka Yasuo,
Shimizu Kikuo
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00689-8
Subject(s) - biology , ubiquitin conjugating enzyme , subfamily , gene , complementary dna , cloning (programming) , ubiquitin , peptide sequence , deubiquitinating enzyme , phylogenetic tree , cdna library , genetics , microbiology and biotechnology , ubiquitin ligase , computer science , programming language
We isolated a 1.7 kb gene (UbcPl) for a ubiquitinconjugating 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 .