An FKBP destabilization domain modulates protein levels in Plasmodium falciparum.
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.
Armstrong
Christopher M
CM
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.
Goldberg
Daniel E
DE
D000818:Animals; D005786:Gene Expression Regulation / Q000502:physiology*; D020868:Gene Silencing; D018390:Gene Targeting / Q000379:methods; D005818:Genetic Engineering / Q000379:methods*; D010963:Plasmodium falciparum / Q000235:genetics*; D017434:Protein Structure, Tertiary; D015800:Protozoan Proteins / Q000737:chemistry / Q000235:genetics*; D022021:Tacrolimus Binding Proteins / Q000737:chemistry / Q000235:genetics*; D014122:Toxoplasma / Q000235:genetics*
D015800:Protozoan Proteins; D022021:Tacrolimus Binding Proteins