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A giant ubiquitin-conjugating enzyme related to IAP apoptosis inhibitors.

http://www.ncbi.nlm.nih.gov/pubmed/9628897

Ubiquitin-conjugating enzymes (UBC) catalyze the covalent attachment of ubiquitin to target proteins and are distinguished by the presence of a UBC domain required for catalysis. Previously identified members of this enzyme family are small proteins and function primarily in selective proteolysis pathways. Here we describe BRUCE (BIR repeat containing ubiquitin-conjugating enzyme), a giant (528-kD) ubiquitin-conjugating enzyme from mice. BRUCE is membrane associated and localizes to the Golgi compartment and the vesicular system. Remarkably, in addition to being an active ubiquitin-conjugating enzyme, BRUCE bears a baculovirus inhibitor of apoptosis repeat (BIR) motif, which to this date has been exclusively found in apoptosis inhibitors of the IAP-related protein family. The BIR motifs of IAP proteins are indispensable for their anti-cell death activity and are thought to function through protein-protein interaction. This suggests that BRUCE may combine properties of IAP-like proteins and ubiquitin-conjugating enzymes and indicates that the family of IAP-like proteins is structurally and functionally more diverse than previously expected.

Pubmed ID: 9628897 RIS Download

Mesh terms: Amino Acid Sequence | Animals | Base Sequence | DNA, Complementary | Gene Expression | Inhibitor of Apoptosis Proteins | Intracellular Membranes | Ligases | Membrane Proteins | Mice | Molecular Sequence Data | PC12 Cells | Rats | Sequence Homology, Amino Acid | Ubiquitin-Conjugating Enzymes | Viral Proteins

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