Definitive evidence for Ufd2-catalyzed elongation of the ubiquitin chain through Lys48 linkage

被引：45

作者：

Saeki, Y

Tayama, Y

Toh-e, A

Yokosawa, H ^{[1
]}

机构：

[1] Hokkaido Univ, Grad Sch Pharmaceut Sci, Dept Biochem, Sapporo, Hokkaido 0600812, Japan

[2] Univ Tokyo, Grad Sch Sci, Dept Biol Sci, Tokyo 1130033, Japan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2004年 / 320卷 / 03期

基金：

日本学术振兴会;

关键词：

ubiquitin; ubiquitinating enzyme; ubiquitin fusion degradation; Ufd2; mass spectrometry; proteolysis;

D O I：

10.1016/j.bbrc.2004.05.216

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：

Saccharomyces cerevisiae Ufd2 is a ubiquitin chain elongation factor in the ubiquitin fusion degradation (UFD) pathway and functions in stress tolerance. A recent study has suggested that the mammalian Ufd2 homologue UFD2a catalyzes formation of Lys27- and Lys33-linked polyubiquitin chains rather than the Lys48-linked chain, but the linkage type of the polyubiquitin chain formed by yeast Ufd2 remains unclear. To determine the property of Ufd2, we reconstituted the UFD pathway using purified enzymes from yeast. Direct determination of the ubiquitin chain linkage type in polyubiquitinated UFD substrates by MALDI-TOF mass spectrometry revealed that Ufd2 catalyzes elongation of the ubiquitin chain through Lys48 linkage. (C) 2004 Elsevier Inc. All rights reserved.

引用

页码：840 / 845

页数：6

共 18 条

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