Purification and characterization of arginyl-tRNA-protein transferase from rabbit reticulocytes. Its involvement in post-translational modification and degradation of …
A Ciechanover, S Ferber, D Ganoth, S Elias… - Journal of Biological …, 1988 - ASBMB
Conjugation of ubiquitin to certain proteins can trigger their degradation. A major question
concerns the structural features of a protein which make it susceptible to ubiquitin ligation.
Recent studies have shown that the selection of proteins for degradation occurs most
probably on a binding site of the ubiquitin-protein ligase (E3). It was shown that a free alpha-
NH2 group is one important feature of the protein structure recognized by the ubiquitin-
ligating enzyme. Proteins with basic or bulky hydrophobic residues in the NH2-terminal …
concerns the structural features of a protein which make it susceptible to ubiquitin ligation.
Recent studies have shown that the selection of proteins for degradation occurs most
probably on a binding site of the ubiquitin-protein ligase (E3). It was shown that a free alpha-
NH2 group is one important feature of the protein structure recognized by the ubiquitin-
ligating enzyme. Proteins with basic or bulky hydrophobic residues in the NH2-terminal …
