[URE3] prion propagation is abolished by a mutation of the primary cytosolic Hsp70 of budding yeast

被引:57
作者
Roberts, BT [1 ]
Moriyama, H [1 ]
Wickner, RB [1 ]
机构
[1] NIDDKD, Lab Biochem & Genet, NIH, Bethesda, MD 20892 USA
关键词
prion; Hsp70; chaperone; genetics; yeast;
D O I
10.1002/yea.1062
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
[URE3] and [PSI+] are infectious protein forms of the Saccharomyces cerevisiae Ure2p and Sup35p, respectively. We isolated an allelle of SSA2, the primary cytosolic Hsp70, in a screen for mutants unable to maintain [URE3]. Designated ssa2-10, the mutation results in a leucine substitution for proline 395, a conserved residue of the peptide-binding domain. This allele also unexpectedly destabilizes [URE3] in newly formed heterozygotes: [URE3] is either absent in heterozygotes formed by crossing wildtype [URE3] cells with ssa2-10 mutants, or present and fully stable. SSA2 deletion mutants are weakly capable of maintaining [URE3]. The ssa2-10 allele is compatible with propagation of [PSI+]. However, in combination with a deletion of SSA1, ssa2-10 eliminates the nonsense-suppression phenotype of [PSI+] cells. Copyright (C) 2003 John Wiley Sons, Ltd.
引用
收藏
页码:107 / 117
页数:11
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