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

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 proteolyt...

Full description

Saved in:
Bibliographic Details
Main Authors: Matuschewski, Kai (Author) , Hauser, Hans-Peter (Author) , Treier, Mathias (Author) , Jentsch, Stefan (Author)
Format: Article (Journal)
Language:English
Published: 1996
In: The journal of biological chemistry
Year: 1996, Volume: 271, Issue: 5, Pages: 2789-2794
ISSN:1083-351X
DOI:10.1074/jbc.271.5.2789
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1074/jbc.271.5.2789
Verlag, lizenzpflichtig, Volltext: https://www.sciencedirect.com/science/article/pii/S0021925817457413
Get full text
Author Notes:Kai Matuschewski, Hans-Peter Hauser, Mathias Treier, and Stefan Jentsch
Description
Summary: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.
Item Description:Gesehen am 08.07.2026
Online verfügbar: 2. Februar 1996, Artikel-Version: 4. Januar 2021
Physical Description:Online Resource
ISSN:1083-351X
DOI:10.1074/jbc.271.5.2789