Burri L, Höckendorff J, Boehm U, Klamp T, Dohmen R J, Lévy F
Ludwig Institute for Cancer Research, Lausanne Branch, University of Lausanne, CH-1066 Epalinges, Switzerland.
Proc Natl Acad Sci U S A. 2000 Sep 12;97(19):10348-53. doi: 10.1073/pnas.190268597.
The assembly of individual mammalian proteasome subunits into catalytically active 20S proteasome is not well understood. Herein, we report the identification and characterization of human and mouse homologues of the yeast proteasome maturating factor Ump1p. We delineate the region of hUMP1 implicated in the specific interaction with proteasome precursors and show that hUMP1 protein is absent from the mature form of the 20S proteasome. We also show that the transcript level of mammalian UMP1 is increased after IFN-gamma treatment and that mammalian UMP1 is functionally related to but not interchangeable with its yeast homologue.
单个哺乳动物蛋白酶体亚基组装成具有催化活性的20S蛋白酶体的过程尚未完全清楚。在此,我们报告了酵母蛋白酶体成熟因子Ump1p的人类和小鼠同源物的鉴定与特性。我们描绘了hUMP1中与蛋白酶体前体特异性相互作用相关的区域,并表明20S蛋白酶体的成熟形式中不存在hUMP1蛋白。我们还表明,γ干扰素处理后哺乳动物UMP1的转录水平升高,并且哺乳动物UMP1在功能上与其酵母同源物相关但不可互换。