Cardiff School of Biosciences, Cardiff University, Park Place, Cardiff, UK.
FEBS Lett. 2011 Jan 3;585(1):139-42. doi: 10.1016/j.febslet.2010.11.026. Epub 2010 Nov 19.
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.
酵母酿酒酵母的 Ddi1 蛋白参与与泛素系统的众多相互作用，这可能是由其 N 端泛素样结构域和 C 端泛素相关结构域介导的。Ddi1 还包含一个具有逆转录病毒天冬氨酸蛋白酶所有特征的中心区域，该区域在细胞周期控制中很重要。在这里，我们证明了该结构域与 N 端区域在蛋白质分泌中的额外作用。这些结果进一步证实了 Ddi1 在体内作为一种具有催化活性的天冬氨酸蛋白酶发挥作用的假说。
