Prion domain initiation of amyloid formation in vitro from native Ure2p

被引:253
作者
Taylor, KL
Cheng, NQ
Williams, RW
Steven, AC
Wickner, RB [1 ]
机构
[1] NIDDKD, Lab Biochem & Genet, NIH, Bethesda, MD 20892 USA
[2] NIAMSD, Struct Biol Lab, NIH, Bethesda, MD 20892 USA
[3] Uniformed Serv Univ Hlth Sci, Dept Biochem & Mol Biol, Bethesda, MD 20814 USA
关键词
D O I
10.1126/science.283.5406.1339
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The [URE3] non-Mendelian genetic element of Saccharomyces cerevisiae is an infectious protein (prion) form of Ure2p, a regulator of nitrogen catabolism. Here, synthetic Ure2p(1-65) were shown to polymerize to form filaments 40 to 45 angstroms in diameter with more than 60 percent beta sheet. Ure2p(1-65) specifically induced full-length native Ure2p to copolymerize under conditions where native Ure2p alone did not polymerize. Like Ure2p in extracts of [URE3] strains, these 180- to 220-angstrom-diameter filaments were protease resistant, The Ure2p(1-65)-Ure2p cofilaments could seed polymerization of native Ure2p to form thicker, Less regular filaments. All filaments stained with Congo Red to produce the green birefringence typical of amyloid. This self-propagating amyloid formation can explain the properties of [URE3].
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页码:1339 / 1343
页数:5
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