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| Item Type: | Article |
|---|---|
| Title: | Identification of a novel family of ubiquitin-conjugating enzymes with distinct amino-terminal extensions |
| Creators Name: | Matuschewski, K., Hauser, H.P., Treier, M. and Jentsch, S. |
| Abstract: | 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 ~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. |
| Keywords: | Amino Acid Sequence, Amino Acid Sequence Homology, Base Sequence, Complementary DNA, Ligases, Molecular Sequence Data, Multigene Family, Phylogeny, Ubiquitins, Animals, Mice |
| Source: | Journal of Biological Chemistry |
| ISSN: | 1083-351X |
| Publisher: | American Society for Biochemistry and Molecular Biology |
| Volume: | 271 |
| Number: | 5 |
| Page Range: | 2789-2794 |
| Date: | 2 February 1996 |
| Official Publication: | https://doi.org/10.1074/jbc.271.5.2789 |
| PubMed: | View item in PubMed |
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