Abstract：
:Proteolysis by the ubiquitin-proteasome pathway is often regulated, but the mechanisms underlying such regulation remain ill-defined. In Saccharomyces cerevisiae, cell type is controlled by the MAT transcription factors. The alpha2 repressor is a known ubiquitin pathway substrate in alpha haploid cells. We show that a1 is rapidly degraded in a haploids. In a/alpha diploids, alpha2 and a1 are stabilized by heterodimerization. Association depends on N-terminal coiled-coil interactions between a1 and alpha2. Residues in alpha2 important for these interactions overlap a critical determinant of an alpha2 degradation signal, which we delimit by extensive mutagenesis. Our data provide a detailed description of a natural ubiquitin-dependent degradation signal and point to a molecular mechanism for regulated turnover in which proteolytic signals are differentially masked in alternative multiprotein complexes.
journal_name
Celljournal_title
Cellauthors
Johnson PR,Swanson R,Rakhilina L,Hochstrasser Mdoi
10.1016/s0092-8674(00)81421-xsubject
Has Abstractpub_date
1998-07-24 00:00:00pages
217-27issue
2eissn
0092-8674issn
1097-4172pii
S0092-8674(00)81421-Xjournal_volume
94pub_type
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