Abstract:
: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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Richter-Ruoff B,Wolf DH,Hochstrasser Mdoi
10.1016/0014-5793(94)01085-4subject
Has Abstractpub_date
1994-10-31 00:00:00pages
50-2issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(94)01085-4journal_volume
354pub_type
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