Cloning of a novel ubiquitin‐conjugating enzyme (E2) gene from the ciliate Paramecium tetraurelia

FEBS Letters

Tokushima, Hideyuki¹  Nakaoka, Yasuo¹  Okano, Satoshi¹  Shimizu, Kikuo² 

[1] Department of Biophysical Engineering, Faculty of Engineering Science, Osaka University, 1-3 Machikaneyama, Toyonaka, Osaka 560, Japan;Radioisotope Research Center, Osaka University, 1-1 Machikaneyama, Toyonaka, Osaka 560, Japan

关键词: Ubiquitin-conjugating enzyme (E2);    cDNA cloning;    Nucleotide sequence;    Phylogenetic tree;    Paramecium tetraurelia;   

DOI  :  10.1016/0014-5793(96)00689-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown