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Journal Article

Identification of a novel family of ubiquitin-conjugating enzymes with distinct amino-terminal extensions


Jentsch,  S
Jentsch Group, Friedrich Miescher Laboratory, Max Planck Society;

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Matuschewski, K., Hauser, H.-P., Treier, M., & Jentsch, S. (1996). Identification of a novel family of ubiquitin-conjugating enzymes with distinct amino-terminal extensions. The Journal of Biological Chemistry, 271(5), 2789-2794. doi:10.1074/jbc.271.5.2789.

Cite as: https://hdl.handle.net/21.11116/0000-000D-1AAB-6
The ubiquitin/proteasome system is the main eukaryotic nonlysosomal protein degradation system. Substrate selectivity of this pathway is thought to be mediated in part by members of a large family of ubiquitin-conjugating (E2) enzymes, which catalyze the covalent attachment of ubiquitin to proteolytic substrates. E2 enzymes have a conserved approximately 150-residue so-called UBC domain, which harbors the cysteine residue required for enzyme-ubiquitin thioester formation. Some E2 enzymes possess additional carboxyl-terminal extensions that are involved in substrate specificity and intracellular localization of the enzyme. Here we describe a novel family of E2 enzymes from higher eukaryotes (Drosophila, mouse, and man) that have amino-terminal extensions but lack carboxyl-terminal extensions. We have identified four different variants of these enzymes that have virtually identical UBC domains (94% identity) but differ in their amino-terminal extensions. In yeast, these enzymes can partially complement mutants deficient in the UBC4 E2 enzyme. This indicates that members of this novel E2 family may operate in UBC4-related proteolytic pathways.