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

被引：21
|
作者：
White, Rhian E. [1 ]
Dickinson, J. Richard [1 ]
Semple, Colin A. M. [2 ]
Powell, David J. [3 ]
Berry, Colin [1 ]
机构：
[1] Cardiff Univ, Cardiff Sch Biosci, Cardiff CF10 3AT, S Glam, Wales
[2] MRC, Human Genet Unit, Inst Genet & Mol Med, Edinburgh EH4 2XU, Midlothian, Scotland
[3] Glaxo SmithKline, Med Res Ctr, Stevenage SG1 2NY, Herts, England
来源：
FEBS LETTERS | 2011年 / 585卷 / 01期
基金：
英国生物技术与生命科学研究理事会;
关键词：
Saccharomyces; Ddi1; VSM1; Protein secretion; Proteinase; Ubiquitin; Aspartic; DAMAGE-INDUCIBLE PROTEINS; HIDDEN MARKOV-MODELS; CELL-CYCLE CONTROL; STRUCTURE PREDICTION; UBIQUITIN RECEPTOR; UBA DOMAINS; YEAST; REGULATOR; HOMOLOGY; BINDING;
D O I：
10.1016/j.febslet.2010.11.026
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
引用
收藏
页码：139 / 142
页数：4
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