Protein dolichylation inPlasmodium falciparum
| Autor: | Emilia A. Kimura, Alejandro M. Katzin, Valnice J. Peres, Fabio Luiz D’Alexandri |
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| Rok vydání: | 2006 |
| Předmět: |
Spectrometry
Mass Electrospray Ionization Plasmodium falciparum Protozoan Proteins Biophysics Protein dolichylation Tandem mass spectrometry Biochemistry chemistry.chemical_compound Dolichol Structural Biology Dolichols Genetics Animals Cysteine Protein prenylation Molecular Biology Polyacrylamide gel electrophoresis Chromatography High Pressure Liquid Protein Synthesis Inhibitors biology Chemistry Proteolytic enzymes Cell Biology biology.organism_classification Covalent bond Chromatography Thin Layer Protein Processing Post-Translational |
| Zdroj: | FEBS Letters. 580:6343-6348 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/j.febslet.2006.10.042 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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