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The retroviral proteinase active site and the N-terminus of Ddi1 are required for repression of protein secretion

White, Rhian Ellen, Dickinson, John Richard, Semple, Colin, Powell, David J. and Berry, Colin 2011. The retroviral proteinase active site and the N-terminus of Ddi1 are required for repression of protein secretion. FEBS Letters 585 (1) , pp. 139-142. 10.1016/j.febslet.2010.11.026

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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.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Biosciences
Subjects: Q Science > QR Microbiology
R Medicine > RB Pathology
Uncontrolled Keywords: Saccharomyces; Ddi1; VSM1; protein secretion; proteinase; ubiquitin; aspartic
Publisher: Elsevier
ISSN: 0014-5793
Last Modified: 06 Mar 2019 20:45
URI: http://orca.cf.ac.uk/id/eprint/19505

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