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An FKBP destabilization domain modulates protein levels in Plasmodium falciparum

descriptionPublicationkeyboard_double_arrow_right Article 11 Nov 2007 English Publisher:Springer Science and Business Media LLCJournal:Nature Methods, volume 4, pages 1,007-1,009 (issn: 1548-7091, eissn: 1548-7105,

Authors: Armstrong, Christopher M.; Goldberg, Daniel E.;

doi: 10.1038/nmeth1132

pmid: 17994030

An FKBP destabilization domain modulates protein levels in Plasmodium falciparum

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Abstract

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.

Related Organizations

University of Mary
United States
Washington State University
United States
Howard Hughes Medical Institute
United States

Keywords

Plasmodium falciparum, Protozoan Proteins, Protein Structure, Tertiary, Tacrolimus Binding Proteins, Gene Expression Regulation, Gene Targeting, Animals, Gene Silencing, Genetic Engineering, Toxoplasma

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	citations This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).	224
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	influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).	Top 1%
	impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.	Top 1%