Protein Dolichylation in Plasmodium Falciparum.
From: Department of Parasitology, Institute of Biomedical Sciences, University of São Paulo, São Paulo, SP, Brazil.
FEBS letters
- Publish Date: Nov 2006
- ISSN: 0014-5793
- Volume: 580
- Issue: 27
- Pages: 6343-8
- Medium: Print
- Language: English
- Citation (JAMA): D'Alexandri Fabio Luiz, Kimura Emilia Akemi, Peres Valnice Jesus, et al. Protein Dolichylation in Plasmodium Falciparum.. FEBS Lett. Nov 2006;580:6343-8
Abstract
We performed reverse-phase thin-layer chromatography and reverse-phase high-performance liquid chromatography (RP-HPLC) analysis of polyisoprenoids released by sulfonium-salt cleavage with methyl iodide from Plasmodium falciparum proteins labeled with [3H]FPP or [3H]GGPP and showed that a dolichol of 11 isoprene units is bound to 21-28-kDa protein clusters from trophozoite and schizont stages. The dolichol structure was confirmed by electrospray-ionization mass spectrometry analysis. Treatment with protein synthesis inhibitors and RP-HPLC analysis of the proteolytic digestion products from parasite proteins labeled with [35S]cysteine and [3H]FPP showed that the attachment of dolichol to protein is a post-translational event and probably occurs via a covalent bond to cysteine residues.
Mesh Headings (Keywords): Animals, Chromatography, High Pressure Liquid, Chromatography, Thin Layer, Cysteine, Dolichol, Plasmodium falciparum, Protein Processing, Post-Translational, Protein Synthesis Inhibitors, Protozoan Proteins, Spectrometry, Mass, Electrospray Ionization
Check for Full Text / PubMed Unique Identifier (PMID): 17084391
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