Cloning of a novel ubiquitin‐conjugating enzyme (E2) gene from the ciliate Paramecium tetraurelia
- 5 August 1996
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 391 (1-2) , 1-4
- https://doi.org/10.1016/0014-5793(96)00689-8
Abstract
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.Keywords
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