PRION-INDUCING DOMAIN OF YEAST URE2P AND PROTEASE RESISTANCE OF URE2P PRION-CONTAINING CELLS
PRION-INDUCING DOMAIN OF YEAST URE2P AND PROTEASE RESISTANCE OF URE2P PRION-CONTAINING CELLS
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DOI：
10.1126/science.270.5233.93
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发表时间：
1995-10-06
期刊：
影响因子：
56.9
通讯作者：
WICKNER, RB
中科院分区：
文献类型：
--
作者：
MASISON, DC;WICKNER, RB
酿酒酵母的[URE3]非孟德尔元件的遗传特性表明，它是一种蛋白质形式的Ure2p，一种氮分解代谢的调节剂。在[URE3]菌株的提取物中，Ure2p与野生型Ure2p相比，对蛋白酶K具有部分抗性。在野生型菌株中过表达Ure2p导致[URE3]产生的频率增加20-200倍，仅过表达Ure2p的氨基末端65个残基就使[URE3]诱导频率增加6000倍。没有这个‘’Prion诱导区‘’，羧基末端的结构域执行了Ure2p的氮素调节功能，但不能改变为[URE3]Prion状态。因此，该结构域在反式中诱导普恩状态，而在顺式中它赋予邻近的氮调节结构域对普恩感染的易感性。
The genetic properties of the [URE3] non-Mendelian element of Saccharomyces cerevisiae suggest that it is a prion (infectious protein) form of Ure2p, a regulator of nitrogen catabolism. In extracts from [URE3] strains, Ure2p was partially resistant to proteinase K compared with Ure2p from wild-type extracts. Overexpression of Ure2p in wild-type strains induced a 20- to 200-fold increase in the frequency with which [URE3] arose, Overexpression of just the amino-terminal 65 residues of Ure2p increased the frequency of [URE3] induction 6000-fold. Without this ''prion-inducing domain'' the carboxyl-terminal domain performed the nitrogen regulation function of Ure2p, but could not be changed to the [URE3] prion state. Thus, this domain induced the prion state in trans, whereas in cis it conferred susceptibility of the adjoining nitrogen regulatory domain to prion infections.