title: The retroviral proteinase active site and the N-terminus of Ddi1 are required for repression of protein secretion.
abstract: The Ddi1 protein of the yeast Saccharomyces cerevisiae is involved in numerous interactions with the ubiquitin system, which may be mediated by its N-terminal ubiquitin like domain and its C-terminal ubiquitin associated domain. Ddi1 also contains a central region with all the features of a retroviral aspartic proteinase, which was shown to be important in cell-cycle control. Here we demonstrate an additional role for this domain, along with the N-terminal region, in protein secretion. These results further substantiate the hypothesis that Ddi1 functions in vivo as a catalytically-active aspartic proteinase.
authors.affiliation: Cardiff School of Biosciences, Cardiff University, Park Place, Cardiff, UK.
authors.forename: Rhian E
authors.initials: RE
authors.lastname: White
authors.forename: J Richard
authors.initials: JR
authors.lastname: Dickinson
authors.forename: Colin A M
authors.initials: CA
authors.lastname: Semple
authors.forename: David J
authors.initials: DJ
authors.lastname: Powell
authors.forename: Colin
authors.initials: C
authors.lastname: Berry
mesh_terms: D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D057055:Aspartic Acid Proteases / Q000235:genetics / Q000378:metabolism*; D015153:Blotting, Western; D020134:Catalytic Domain; D008969:Molecular Sequence Data; D009154:Mutation; D021381:Protein Transport; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism*; D055571:Secretory Pathway
chemical_list: C108125:DDI1 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D057055:Aspartic Acid Proteases