Rad23 provides a link between the Png1 deglycosylating enzyme and the 26 S proteasome in yeast

被引:99
作者
Suzuki, T
Park, H
Kwofie, MA
Lennarz, WJ [1 ]
机构
[1] SUNY Stony Brook, Dept Biochem & Cell Biol, Stony Brook, NY 11794 USA
[2] SUNY Stony Brook, Inst Cell & Dev Biol, Stony Brook, NY 11794 USA
关键词
D O I
10.1074/jbc.M100826200
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
In addition to a role in DNA repair events in yeast, several lines of evidence indicate that the Rad23 protein (Rad23p) may regulate the activity of the 26 S proteasome. We report evidence that a de-N-glycosylating enzyme, Png1p, may be involved in the proteasomal degradation pathway via its binding to Rad23p. Interaction of Rad23p and Png1p was first detected by two-hybrid screening, and this interaction in vivo was confirmed by biochemical analyses. The Png1p-Rad23p complex was shown to be distinct from the well established DNA repair complex, Rad4p-Rad23p. We propose a model in which Rad23p functions as an escort protein to link the 26 S proteasome with proteins such as Rad4p or Png1p to regulate their cellular activities.
引用
收藏
页码:21601 / 21607
页数:7
相关论文
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