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 ORCID: https://orcid.org/0000-0002-9943-548X 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:	19 Oct 2022 08:55
URI:	https://orca.cardiff.ac.uk/id/eprint/19505

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