The ubiquitin-like protein HUB1 forms SDS-resistant complexes with cellular proteins in the absence of ATP.

Abstract

Ubiquitin and ubiquitin-like modifiers (UBLs) form covalent complexes with other proteins by isopeptide formation between their carboxyl (C)-termini and epsilon-amino groups of lysine residues of acceptor proteins. A hallmark of UBLs is a protruding C-terminal tail with a terminal glycine residue, which is required for ATP-dependent conjugation. Recently… (More)

Topics

Cite this paper

@article{Lders2003TheUP, title={The ubiquitin-like protein HUB1 forms SDS-resistant complexes with cellular proteins in the absence of ATP.}, author={Jens L{\"u}ders and George Pyrowolakis and Stefan Jentsch}, journal={EMBO reports}, year={2003}, volume={4 12}, pages={1169-74} }