An FKBP destabilization domain modulates protein levels in Plasmodium falciparum

被引：182

作者：

Armstrong, Christopher M. ^{[1
]}

Goldberg, Daniel E. ^{[1
]}

机构：

[1] Washington Univ, Sch Med, Howard Hughes Med Inst, Dept Mol Microbiol & Med, St Louis, MO 63110 USA

来源：

NATURE METHODS | 2007年 / 4卷 / 12期

关键词：

D O I：

10.1038/nmeth1132

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

To enhance the repertoire of molecular tools for studying malaria parasite biology, we adapted a ligand-regulatable FKBP protein destabilization domain (ddFKBP) for use in P. falciparum. We destabilized the reporter yellow fluorescent protein (YFP) and the P. falciparum protease falcipain-2 in a ligand-reversible manner by tagging with ddFKBP. The swollen food vacuole phenotype of falcipain-2 knockout parasites could be rescued in a Shld1 ligand-dependent fashion by falcipain-2-ddFKBP expression.

引用

页码：1007 / 1009

页数：3

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