Inhibition of ubiquitin-dependent proteolysis by des-Gly-Gly-ubiquitin: Implications for the mechanism of polyubiquitin synthesis Academic Article uri icon

Overview

MeSH Major

  • Phospholipid Transfer Proteins

abstract

  • Cleavage of the two carboxyl-terminal glycine residues from native ubiquitin yields the proteolysis-incompetent derivative des-Gly-Gly-ubiquitin. We report here that this derivative inhibits the ATP-dependent degradation of casein and is multi-ubiquitinated but not degraded by reticulocyte lysates. Inhibition of proteolysis diminished with increasing concentration of native ubiquitin, but was not reduced by increased casein concentration. Cleavage of the last four residues from ubiquitin yielded a derivative that was a weaker inhibitor of proteolysis and a poorer substrate for ubiquitination. These results suggest that the conjugation of ubiquitin to ubiquitin during polyubiquitin synthesis involves a specific conjugation system that recognizes ubiquitin and some of its derivatives, but not general proteolysis substrates, as ubiquitin acceptors.

publication date

  • July 14, 1989

Research

keywords

  • Academic Article

Identity

Digital Object Identifier (DOI)

  • 10.1016/0006-291X(89)91966-9

Additional Document Info

start page

  • 89

end page

  • 94

volume

  • 162

number

  • 1