Characterization of an eukaryotic peptide deformylase from Plasmodium falciparum
Abbreviated Journal Title
Arch. Biochem. Biophys.
peptide deformylase; eukaryotes; parasite; inhibition; catalysis; antimalarial target; apicoplast; ESCHERICHIA-COLI; SPECTROPHOTOMETRIC ASSAY; POLYPEPTIDE DEFORMYLASE; NEW-GENERATION; ACTIVE-SITE; PROTEIN; AGENTS; IRON; IDENTIFICATION; TRANSLATION; Biochemistry & Molecular Biology; Biophysics
Ribosomal protein synthesis in eubacteria and eukaryotic organelles initiates with an N-formylmethionyl-tRNA(i), resulting in N-terminal formylation of all nascent polypeptides. Peptide deformylase (PDF) catalyzes the subsequent removal of the N-terminal formyl group from the majority of bacterial proteins. Until recently, PDF has been thought as an enzyme unique to the bacterial kingdom. Searches of the genomic DNA databases identified several genes that encode proteins of high sequence homology to bacterial PDF from eukaryotic organisms. The cDNA encoding Plasmodium falciparum PDF (PfPDF) has been cloned and overexpressed in Escherichia coli. The recombinant protein is catalytically active in deformylating N-formylated peptides, shares many of the properties of bacterial PDF, and is inhibited by specific PDF inhibitors. Western blot analysis indicated expression of mature PfPDF in trophozoite, schizont, and segmenter stages of intraerythrocytic development. These results provide strong evidence that a functional PDF is present in P. falciparum. In addition, PDF inhibitors inhibited the growth of P. falciparum in the intraerythrocytic culture. (C) 2001 Elsevier Science.
Archives of Biochemistry and Biophysics
"Characterization of an eukaryotic peptide deformylase from Plasmodium falciparum" (2001). Faculty Bibliography 2000s. 2940.