Trypanosoma cruzi amino acid transporter TcAAAP411 mediates arginine uptake in yeasts
Trypanosoma cruzi, the aetiological agent of Chagas' disease, is exposed to extremely different environment conditions during its life cycle, and transporters are key molecules for its adaptive regulation. Amino acids, and particularly arginine, are essential components in T. cruzi metabolism....
| Autores: | , , , , , , |
|---|---|
| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2010 |
| País: | Argentina |
| Institución: | Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales |
| Repositorio: | Biblioteca Digital (UBA-FCEN) |
| Idioma: | inglés |
| OAI Identifier: | paperaa:paper_03781097_v306_n2_p97_Carrillo |
| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_03781097_v306_n2_p97_Carrillo |
| Access Level: | acceso abierto |
| Palabra clave: | AAAP family Amino acid transport Arginine permease Chagas' disease Trypanosoma cruzi arginine arginine permease auxin permease bacterial enzyme canavanine unclassified drug active transport amino acid transport amino terminal sequence article bacterial strain binding affinity carboxy terminal sequence controlled study expression vector gene identification genetic analysis nonhuman parasite identification parasite migration priority journal sensitivity and specificity transport kinetics yeast Amino Acid Transport Systems, Basic Arginine Genetic Complementation Test Protozoan Proteins Recombinant Proteins Saccharomyces cerevisiae |
| Sumario: | Trypanosoma cruzi, the aetiological agent of Chagas' disease, is exposed to extremely different environment conditions during its life cycle, and transporters are key molecules for its adaptive regulation. Amino acids, and particularly arginine, are essential components in T. cruzi metabolism. In this work, a novel T. cruzi arginine permease was identified by screening different members of the AAAP family (amino acid/auxin permeases) in yeast complementation assays using a toxic arginine analogue. One gene candidate, TcAAAP411, was characterized as a very specific, high-affinity, l-arginine permease. This work is the first identification of the molecular components involved specifically in amino acid transport in T. cruzi and provides new insights for further validation of the TcAAAP family as functional permeases. © 2010 Federation of European Microbiological Societies. |
|---|