Dual acylation accounts for the localization of {alpha}19-giardin in the ventral flagellum pair of Giardia lamblia
| Autor: | Verena Kluempers, Daniela Niebur, Mirela Šarić, Henning Scholze, Anke Vahrmann, Adrian B. Hehl |
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| Přispěvatelé: | University of Zurich, Scholze, H |
| Rok vydání: | 2009 |
| Předmět: |
10078 Institute of Parasitology
Protein family Acylation Protozoan Proteins 610 Medicine & health Flagellum medicine.disease_cause Microbiology 03 medical and health sciences Palmitoylation 600 Technology medicine 1312 Molecular Biology Giardia lamblia Molecular Biology 030304 developmental biology Myristoylation 0303 health sciences Microscopy Confocal biology 030302 biochemistry & molecular biology 2404 Microbiology General Medicine Articles Cell biology Cytoskeletal Proteins Tubulin Biochemistry Flagella biology.protein 570 Life sciences lipids (amino acids peptides and proteins) Heterologous expression Lipid modification |
| Zdroj: | Eukaryotic cell |
| DOI: | 10.1128/EC.00136-09 |
| Popis: | A Giardia -specific protein family denominated as α-giardins, represents the major protein component, besides tubulin, of the cytoskeleton of the human pathogenic parasite Giardia lamblia . One of its members, α19-giardin, carries an N-terminal sequence extension of MGCXXS, which in many proteins serves as a target for dual lipid conjugation: myristoylation at the glycine residue after removal of the methionine and palmitoylation at the cysteine residue. As the first experimental evidence of a lipid modification, we found α19-giardin to be associated with the membrane fraction of disrupted trophozoites. After heterologous coexpression of α19-giardin with giardial N -myristoyltransferase (NMT) in E scherichia coli , we found the protein in a myristoylated form. Additionally, after heterologous expression together with the palmitoyl transferase Pfa3 in Saccharomyces cerevisiae , α19-giardin associates with the membrane of the main vacuole. Immunocytochemical colocalization studies on wild-type Giardia trophozoites with tubulin provide evidence that α19-giardin exclusively localizes to the ventral pair of the giardial flagella. A mutant in which the putatively myristoylated N-terminal glycine residue was replaced by alanine lost this specific localization. Our findings suggest that the dual lipidation of α19-giardin is responsible for its specific flagellar localization. |
| Databáze: | OpenAIRE |
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