| Título: | The Leishmania donovani peroxin 14 N-terminal region is important for glycosomal localization |
| Autores: | Nyisztor, Michael. |
| Fecha: | 2007 |
| Publicador: | McGill University - MCGILL |
| Fuente: |
 |
| Tipo: | Electronic Thesis or Dissertation |
| Tema: |
Leishmania. Microbodies. |
| Descripción: |
Glycosomes are subcellular organelles that are evolutionarily related to the peroxisomes of higher eukaryotes. The Leishmania glycosome performs various metabolic processes that are essential for the survival of these parasites, such as the glycolytic process. Proteins that are destined for import into the glycosome interact selectively with specific cytosolic receptors peroxin 5(PEX5) or PEX7. The PEX5-protein complex migrates toward the glycosomal membrane where it interacts with PEX14, a vital step for protein important into the glycosome. This project investigated the interaction mechanism of Leishmania donovani PEX14 with the glycosomal membrane. The regions responsible for PEX14 interaction with the glycosomal membrane are established in higher eukaryotes. LdPEX14 is poorly conserved with respect to the other PEX14 homologues. In Leishmania the interaction of LdPEX14 with the glycsomal membrane has been shown to be unique in terms of its lack of insertion in the glycosomal membrane. Using LdPEX14 mutants it was determined that the first 63 amino acids are important for the interaction of LdPEX14 with the glycosomal membrane. Results further suggest that LdPEX14 is a homopolymer forming a complex of 20S in size which is vital for the proper functioning of the glycosome. |
| Idioma: | en |
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