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

Rhian E White, J Richard Dickinson, Colin A M Semple, David J Powell, Colin Berry

Research output: Contribution to journalArticlepeer-review

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.
Original languageEnglish
Pages (from-to)139-42
Number of pages4
JournalFEBS Letters
Volume585
Issue number1
DOIs
Publication statusPublished - 2011

Keywords

  • Saccharomyces cerevisiae
  • Ddi1
  • VSM1
  • Protein secretion
  • Proteinase
  • Ubiquitin
  • Aspartic

Fingerprint Dive into the research topics of 'The retroviral proteinase active site and the N-terminus of Ddi1 are required for repression of protein secretion'. Together they form a unique fingerprint.

Cite this