Trypanosoma cruzi amino acid transporter TcAAAP411 mediates arginine uptake in yeasts

Autores
Carrillo, C.; Canepa, G.E.; Giacometti, A.; Bouvier, L.A.; Miranda, M.R.; De Los Milagros Camara, M.; Pereira, C.A.
Año de publicación
2010
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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.
Fil:Carrillo, C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Canepa, G.E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Bouvier, L.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:De Los Milagros Camara, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Pereira, C.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fuente
FEMS Microbiol. Lett. 2010;306(2):97-102
Materia
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
Trypanosoma cruzi
yeast
Amino Acid Transport Systems, Basic
Arginine
Genetic Complementation Test
Protozoan Proteins
Recombinant Proteins
Saccharomyces cerevisiae
Trypanosoma cruzi
Trypanosoma cruzi
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/2.5/ar
Repositorio
Biblioteca Digital (UBA-FCEN)
Institución
Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
OAI Identificador
paperaa:paper_03781097_v306_n2_p97_Carrillo
Acceder
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oai_identifier_str paperaa:paper_03781097_v306_n2_p97_Carrillo
network_acronym_str BDUBAFCEN
repository_id_str 1896
network_name_str Biblioteca Digital (UBA-FCEN)
spelling Trypanosoma cruzi amino acid transporter TcAAAP411 mediates arginine uptake in yeastsCarrillo, C.Canepa, G.E.Giacometti, A.Bouvier, L.A.Miranda, M.R.De Los Milagros Camara, M.Pereira, C.A.AAAP familyAmino acid transportArginine permeaseChagas' diseaseTrypanosoma cruziargininearginine permeaseauxin permeasebacterial enzymecanavanineunclassified drugactive transportamino acid transportamino terminal sequencearticlebacterial strainbinding affinitycarboxy terminal sequencecontrolled studyexpression vectorgene identificationgenetic analysisnonhumanparasite identificationparasite migrationpriority journalsensitivity and specificitytransport kineticsTrypanosoma cruziyeastAmino Acid Transport Systems, BasicArginineGenetic Complementation TestProtozoan ProteinsRecombinant ProteinsSaccharomyces cerevisiaeTrypanosoma cruziTrypanosoma cruziTrypanosoma 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.Fil:Carrillo, C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Canepa, G.E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Bouvier, L.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:De Los Milagros Camara, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Pereira, C.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.2010info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12110/paper_03781097_v306_n2_p97_CarrilloFEMS Microbiol. Lett. 2010;306(2):97-102reponame:Biblioteca Digital (UBA-FCEN)instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesinstacron:UBA-FCENenginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/2.5/ar2025-09-29T13:42:57Zpaperaa:paper_03781097_v306_n2_p97_CarrilloInstitucionalhttps://digital.bl.fcen.uba.ar/Universidad públicaNo correspondehttps://digital.bl.fcen.uba.ar/cgi-bin/oaiserver.cgiana@bl.fcen.uba.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:18962025-09-29 13:42:58.606Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesfalse
dc.title.none.fl_str_mv Trypanosoma cruzi amino acid transporter TcAAAP411 mediates arginine uptake in yeasts
title Trypanosoma cruzi amino acid transporter TcAAAP411 mediates arginine uptake in yeasts
spellingShingle Trypanosoma cruzi amino acid transporter TcAAAP411 mediates arginine uptake in yeasts
Carrillo, C.
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
Trypanosoma cruzi
yeast
Amino Acid Transport Systems, Basic
Arginine
Genetic Complementation Test
Protozoan Proteins
Recombinant Proteins
Saccharomyces cerevisiae
Trypanosoma cruzi
Trypanosoma cruzi
title_short Trypanosoma cruzi amino acid transporter TcAAAP411 mediates arginine uptake in yeasts
title_full Trypanosoma cruzi amino acid transporter TcAAAP411 mediates arginine uptake in yeasts
title_fullStr Trypanosoma cruzi amino acid transporter TcAAAP411 mediates arginine uptake in yeasts
title_full_unstemmed Trypanosoma cruzi amino acid transporter TcAAAP411 mediates arginine uptake in yeasts
title_sort Trypanosoma cruzi amino acid transporter TcAAAP411 mediates arginine uptake in yeasts
dc.creator.none.fl_str_mv Carrillo, C.
Canepa, G.E.
Giacometti, A.
Bouvier, L.A.
Miranda, M.R.
De Los Milagros Camara, M.
Pereira, C.A.
author Carrillo, C.
author_facet Carrillo, C.
Canepa, G.E.
Giacometti, A.
Bouvier, L.A.
Miranda, M.R.
De Los Milagros Camara, M.
Pereira, C.A.
author_role author
author2 Canepa, G.E.
Giacometti, A.
Bouvier, L.A.
Miranda, M.R.
De Los Milagros Camara, M.
Pereira, C.A.
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv 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
Trypanosoma cruzi
yeast
Amino Acid Transport Systems, Basic
Arginine
Genetic Complementation Test
Protozoan Proteins
Recombinant Proteins
Saccharomyces cerevisiae
Trypanosoma cruzi
Trypanosoma cruzi
topic 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
Trypanosoma cruzi
yeast
Amino Acid Transport Systems, Basic
Arginine
Genetic Complementation Test
Protozoan Proteins
Recombinant Proteins
Saccharomyces cerevisiae
Trypanosoma cruzi
Trypanosoma cruzi
dc.description.none.fl_txt_mv 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.
Fil:Carrillo, C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Canepa, G.E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Bouvier, L.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:De Los Milagros Camara, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Pereira, C.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
description 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.
publishDate 2010
dc.date.none.fl_str_mv 2010
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/20.500.12110/paper_03781097_v306_n2_p97_Carrillo
url http://hdl.handle.net/20.500.12110/paper_03781097_v306_n2_p97_Carrillo
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/2.5/ar
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/2.5/ar
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv FEMS Microbiol. Lett. 2010;306(2):97-102
reponame:Biblioteca Digital (UBA-FCEN)
instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron:UBA-FCEN
reponame_str Biblioteca Digital (UBA-FCEN)
collection Biblioteca Digital (UBA-FCEN)
instname_str Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron_str UBA-FCEN
institution UBA-FCEN
repository.name.fl_str_mv Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
repository.mail.fl_str_mv ana@bl.fcen.uba.ar
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