[HTML][HTML] Lactacystin and clasto-lactacystin β-lactone modify multiple proteasome β-subunits and inhibit intracellular protein degradation and major histocompatibility …
A Craiu, M Gaczynska, T Akopian, CF Gramm… - Journal of Biological …, 1997 - ASBMB
The antibiotic lactacystin was reported to covalently modify β-subunit X of the mammalian 20
S proteasome and inhibit several of its peptidase activities. However, we demonstrate that [3
H] lactacystin treatment modifies all the proteasome's catalytic β-subunits. Lactacystin and its
more potent derivative β-lactone irreversibly inhibit protein breakdown and the chymotryptic,
tryptic, and peptidylglutamyl activities of purified 20 S and 26 S particles, although at
different rates. Exposure to these agents for 1 to 2 h reduced the degradation of short-and …
S proteasome and inhibit several of its peptidase activities. However, we demonstrate that [3
H] lactacystin treatment modifies all the proteasome's catalytic β-subunits. Lactacystin and its
more potent derivative β-lactone irreversibly inhibit protein breakdown and the chymotryptic,
tryptic, and peptidylglutamyl activities of purified 20 S and 26 S particles, although at
different rates. Exposure to these agents for 1 to 2 h reduced the degradation of short-and …