Characterization of Trypanosoma brucei PEX14 and its role in the import of glycosomal matrix proteins
| Autor: | Jungwoo Choe, Frank Voncken, Wim G. J. Hol, Abhinav Kumar, Paul A.M. Michels, Juliette Moyersoen |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
Peroxisome-Targeting Signal 1 Receptor
Molecular Sequence Data Trypanosoma brucei brucei Protozoan Proteins Receptors Cytoplasmic and Nuclear Digitonin Peroxin Trypanosoma brucei Cell Fractionation Microbodies Biochemistry Glycosome Protein–protein interaction Animals Microbody biology Membrane Proteins biology.organism_classification Immunohistochemistry Recombinant Proteins Cell biology Transport protein Protein Transport Cytosol Membrane protein Indicators and Reagents RNA Interference |
| Zdroj: | European Journal of Biochemistry. 270:2059-2067 |
| ISSN: | 1432-1033 0014-2956 |
| DOI: | 10.1046/j.1432-1033.2003.03582.x |
| Popis: | It has been shown previously in various organisms that the peroxin PEX14 is a component of a docking complex at the peroxisomal membrane, where it is involved in the import of matrix proteins into the organelle after their synthesis in the cytosol and recognition by a receptor. Here we present a characterization of the Trypanosoma brucei homologue of PEX14. It is shown that the protein is associated with glycosomes, the peroxisome-like organelles of trypanosomatids in which most glycolytic enzymes are compartmentalized. The N-terminal part of the protein binds specifically to TbPEX5, the cytosolic receptor for glycosomal matrix proteins with a peroxisome-targeting signal type 1 (PTS-1). TbPEX14 mRNA depletion by RNA interference results, in both bloodstream-form and procyclic, insect-stage T. brucei, in mislocalization of glycosomal proteins to the cytosol. The mislocalization was observed for different classes of matrix proteins: proteins with a C-terminal PTS-1, a N-terminal PTS-2 and a polypeptide internal I-PTS. The RNA interference experiments also showed that TbPEX14 is essential for the survival of bloodstream-form and procyclic trypanosomes. These data indicate the protein's great potential as a target for selective trypanocidal drugs. |
| Databáze: | OpenAIRE |
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