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The retroviral proteinase active site and the N‐terminus of Ddi1 are required for repression of protein secretion
Author(s) -
White Rhian E.,
Dickinson J. Richard,
Semple Colin A.M.,
Powell David J.,
Berry Colin
Publication year - 2011
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.11.026
Subject(s) - ubiquitin , saccharomyces cerevisiae , secretion , microbiology and biotechnology , yeast , biochemistry , biology , psychological repression , chemistry , gene , gene expression
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.