Nat Methods. 2007 Dec;4(12):1007-9. Epub 2007 Nov 11.

An FKBP destabilization domain modulates protein levels in Plasmodium falciparum.

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Howard Hughes Medical Institute, Washington University School of Medicine, Departments of Molecular Microbiology and Medicine, 660 S. Euclid Ave., Box 8230, St. Louis, Missouri 63110, USA.

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.

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Nat Methods. 2007 Dec;4(12):999-1000.

PMID:: 17994030; [PubMed - indexed for MEDLINE]

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Research Support, N.I.H., Extramural

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AI47798/AI/NIAID NIH HHS/United States

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