Suzuki T, Park H, Kwofie M A, Lennarz W J
Department of Biochemistry, Institute for Cell and Developmental Biology, State University of New York at Stony Brook, Stony Brook, New York 11794-5215, USA.
J Biol Chem. 2001 Jun 15;276(24):21601-7. doi: 10.1074/jbc.M100826200. Epub 2001 Mar 20.
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.
除了在酵母的DNA修复事件中发挥作用外，几条证据表明Rad23蛋白（Rad23p）可能调节26S蛋白酶体的活性。我们报告了证据表明一种去N-糖基化酶Png1p可能通过与Rad23p结合而参与蛋白酶体降解途径。Rad23p和Png1p的相互作用首先通过双杂交筛选检测到，并且这种体内相互作用通过生化分析得到证实。Png1p-Rad23p复合物被证明与已确立的DNA修复复合物Rad4p-Rad23p不同。我们提出了一个模型，其中Rad23p作为一种护送蛋白，将26S蛋白酶体与诸如Rad4p或Png1p等蛋白质连接起来，以调节它们的细胞活性。
