التفاصيل البيبلوغرافية
العنوان: |
The retroviral proteinase active site and the N-terminus of Ddi1 are required for repression of protein secretion |
المؤلفون: |
White, Rhian E.1, Dickinson, J. Richard1, Semple, Colin A.M.2, Powell, David J.3, Berry, Colin1 Berry@cf.ac.uk |
المصدر: |
FEBS Letters. Jan2011, Vol. 585 Issue 1, p139-142. 4p. |
مصطلحات موضوعية: |
*PROTEINASES, *SECRETION, *SACCHAROMYCES cerevisiae, *UBIQUITIN, *CELL cycle, *ASPARTIC proteinases, *BINDING sites |
مستخلص: |
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. [ABSTRACT FROM AUTHOR] |
قاعدة البيانات: |
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