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http://purl.uniprot.org/citations/9695950http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9695950http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9695950http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/9695950http://purl.org/dc/terms/identifier"doi:10.1016/s0092-8674(00)81421-x"xsd:string
http://purl.uniprot.org/citations/9695950http://purl.org/dc/terms/identifier"doi:10.1016/s0092-8674(00)81421-x"xsd:string
http://purl.uniprot.org/citations/9695950http://purl.uniprot.org/core/author"Johnson P.R."xsd:string
http://purl.uniprot.org/citations/9695950http://purl.uniprot.org/core/author"Johnson P.R."xsd:string
http://purl.uniprot.org/citations/9695950http://purl.uniprot.org/core/author"Swanson R."xsd:string
http://purl.uniprot.org/citations/9695950http://purl.uniprot.org/core/author"Swanson R."xsd:string
http://purl.uniprot.org/citations/9695950http://purl.uniprot.org/core/author"Hochstrasser M."xsd:string
http://purl.uniprot.org/citations/9695950http://purl.uniprot.org/core/author"Hochstrasser M."xsd:string
http://purl.uniprot.org/citations/9695950http://purl.uniprot.org/core/author"Rakhilina L."xsd:string
http://purl.uniprot.org/citations/9695950http://purl.uniprot.org/core/author"Rakhilina L."xsd:string
http://purl.uniprot.org/citations/9695950http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9695950http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9695950http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/9695950http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/9695950http://purl.uniprot.org/core/pages"217-227"xsd:string
http://purl.uniprot.org/citations/9695950http://purl.uniprot.org/core/pages"217-227"xsd:string
http://purl.uniprot.org/citations/9695950http://purl.uniprot.org/core/title"Degradation signal masking by heterodimerization of MATalpha2 and MATa1 blocks their mutual destruction by the ubiquitin-proteasome pathway."xsd:string
http://purl.uniprot.org/citations/9695950http://purl.uniprot.org/core/title"Degradation signal masking by heterodimerization of MATalpha2 and MATa1 blocks their mutual destruction by the ubiquitin-proteasome pathway."xsd:string
http://purl.uniprot.org/citations/9695950http://purl.uniprot.org/core/volume"94"xsd:string
http://purl.uniprot.org/citations/9695950http://purl.uniprot.org/core/volume"94"xsd:string
http://purl.uniprot.org/citations/9695950http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9695950
http://purl.uniprot.org/citations/9695950http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9695950