Degradation of the yeast MAT alpha 2 transcriptional regulator is mediated by the proteasome.
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.
Institut für Biochemie, Universität Stuttgart, Germany.
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Richter-Ruoff
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Wolf
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Hochstrasser
D003546:Cysteine Endopeptidases / Q000235:genetics / Q000378:metabolism*; D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism*; D018398:Homeodomain Proteins; D009097:Multienzyme Complexes / Q000235:genetics / Q000378:metabolism*; D009154:Mutation / Q000502:physiology; D046988:Proteasome Endopeptidase Complex; D012097:Repressor Proteins / Q000235:genetics / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins
D005656:Fungal Proteins; D018398:Homeodomain Proteins; C062928:MATA2 protein, S cerevisiae; D009097:Multienzyme Complexes; D012097:Repressor Proteins; D029701:Saccharomyces cerevisiae Proteins; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex