Rapid degradation of specific regulatory proteins plays a role in a wide range of cellular phenomena, including cell cycle progression and the regulation of cell growth and differentiation. A major mechanism of selective protein turnover in vivo involves a large multi-subunit protease known as the proteasome or multi-catalytic proteinase. At the same time, the degradation of many cellular proteins requires their covalent ligation to the polypeptide ubiquitin. Here we show that the yeast S. cerevisiae MAT alpha 2 repressor, which is known to be ubiquitinylated in vivo, requires the proteasome for its rapid intracellular proteolysis.

• PMID: 7957900
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Reference Type

Journal Article | Research Support, Non-U.S. Gov't

Authors

Richter-Ruoff B, Wolf DH, Hochstrasser M

Primary Lit For

MATALPHA2 | HMLALPHA2

Additional Lit For

Review For