Acidic ribosomal P proteins are phosphorylated in Trypanosoma cruzi

Autores
Gomez, Eliana B.; Medina, Gabriel; Ballesta, Juan P. G.; Levin, Mariano Jorge; Tellez, Maria Teresa
Año de publicación
2001
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Trypanosoma cruzi ribosomes from epimastigote forms were purified as determined by electron microscopy and isoelectrofocusing was used to analyse this purified ribosome fraction. Silver stained gels revealed that acidic proteins are present in at least 10 different isoforms, in accord with previous cloning studies. To detect phosphorylation, in vitro phosphorylation assays using the recombinant protein TcP2β-mbp were carried out. The results showed that T. cruzi cytosolic fraction possesses protein kinase activity able to phosphorylate the recombinant protein. Purified ribosomes contain protein kinases that could also phosphorylate the recombinant protein TcP2β-mbp. Labelling parasites with [32Pi] in a phosphate free medium demonstrated that ribosome proteins, recognised with a specific mouse antiserum against recombinant TcP2β proteins, are phosphorylated in vivo. All these results suggest that in vivo phosphorylation of ribosome TcP2β proteins are mediated by protein kinase(s) not yet identified.
Fil: Gomez, Eliana B.. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Medina, Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Ballesta, Juan P. G.. Universidad Autónoma de Madrid; España
Fil: Levin, Mariano Jorge. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Tellez, Maria Teresa. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina
Materia
Isoelectrofocusing
P Proteins
Protein Phosphorylation
Ribosome
Trypanosoma
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/79331
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/79331
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Acidic ribosomal P proteins are phosphorylated in Trypanosoma cruziGomez, Eliana B.Medina, GabrielBallesta, Juan P. G.Levin, Mariano JorgeTellez, Maria TeresaIsoelectrofocusingP ProteinsProtein PhosphorylationRibosomeTrypanosomahttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Trypanosoma cruzi ribosomes from epimastigote forms were purified as determined by electron microscopy and isoelectrofocusing was used to analyse this purified ribosome fraction. Silver stained gels revealed that acidic proteins are present in at least 10 different isoforms, in accord with previous cloning studies. To detect phosphorylation, in vitro phosphorylation assays using the recombinant protein TcP2β-mbp were carried out. The results showed that T. cruzi cytosolic fraction possesses protein kinase activity able to phosphorylate the recombinant protein. Purified ribosomes contain protein kinases that could also phosphorylate the recombinant protein TcP2β-mbp. Labelling parasites with [32Pi] in a phosphate free medium demonstrated that ribosome proteins, recognised with a specific mouse antiserum against recombinant TcP2β proteins, are phosphorylated in vivo. All these results suggest that in vivo phosphorylation of ribosome TcP2β proteins are mediated by protein kinase(s) not yet identified.Fil: Gomez, Eliana B.. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; ArgentinaFil: Medina, Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; ArgentinaFil: Ballesta, Juan P. G.. Universidad Autónoma de Madrid; EspañaFil: Levin, Mariano Jorge. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; ArgentinaFil: Tellez, Maria Teresa. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; ArgentinaElsevier2001-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/79331Gomez, Eliana B.; Medina, Gabriel; Ballesta, Juan P. G.; Levin, Mariano Jorge; Tellez, Maria Teresa; Acidic ribosomal P proteins are phosphorylated in Trypanosoma cruzi; Elsevier; International Journal for Parasitology; 31; 10; 12-2001; 1032-10390020-7519CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0020751901002193info:eu-repo/semantics/altIdentifier/doi/10.1016/S0020-7519(01)00219-3info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:06:42Zoai:ri.conicet.gov.ar:11336/79331instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-15 15:06:43.241CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Acidic ribosomal P proteins are phosphorylated in Trypanosoma cruzi
title Acidic ribosomal P proteins are phosphorylated in Trypanosoma cruzi
spellingShingle Acidic ribosomal P proteins are phosphorylated in Trypanosoma cruzi
Gomez, Eliana B.
Isoelectrofocusing
P Proteins
Protein Phosphorylation
Ribosome
Trypanosoma
title_short Acidic ribosomal P proteins are phosphorylated in Trypanosoma cruzi
title_full Acidic ribosomal P proteins are phosphorylated in Trypanosoma cruzi
title_fullStr Acidic ribosomal P proteins are phosphorylated in Trypanosoma cruzi
title_full_unstemmed Acidic ribosomal P proteins are phosphorylated in Trypanosoma cruzi
title_sort Acidic ribosomal P proteins are phosphorylated in Trypanosoma cruzi
dc.creator.none.fl_str_mv Gomez, Eliana B.
Medina, Gabriel
Ballesta, Juan P. G.
Levin, Mariano Jorge
Tellez, Maria Teresa
author Gomez, Eliana B.
author_facet Gomez, Eliana B.
Medina, Gabriel
Ballesta, Juan P. G.
Levin, Mariano Jorge
Tellez, Maria Teresa
author_role author
author2 Medina, Gabriel
Ballesta, Juan P. G.
Levin, Mariano Jorge
Tellez, Maria Teresa
author2_role author
author
author
author
dc.subject.none.fl_str_mv Isoelectrofocusing
P Proteins
Protein Phosphorylation
Ribosome
Trypanosoma
topic Isoelectrofocusing
P Proteins
Protein Phosphorylation
Ribosome
Trypanosoma
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Trypanosoma cruzi ribosomes from epimastigote forms were purified as determined by electron microscopy and isoelectrofocusing was used to analyse this purified ribosome fraction. Silver stained gels revealed that acidic proteins are present in at least 10 different isoforms, in accord with previous cloning studies. To detect phosphorylation, in vitro phosphorylation assays using the recombinant protein TcP2β-mbp were carried out. The results showed that T. cruzi cytosolic fraction possesses protein kinase activity able to phosphorylate the recombinant protein. Purified ribosomes contain protein kinases that could also phosphorylate the recombinant protein TcP2β-mbp. Labelling parasites with [32Pi] in a phosphate free medium demonstrated that ribosome proteins, recognised with a specific mouse antiserum against recombinant TcP2β proteins, are phosphorylated in vivo. All these results suggest that in vivo phosphorylation of ribosome TcP2β proteins are mediated by protein kinase(s) not yet identified.
Fil: Gomez, Eliana B.. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Medina, Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Ballesta, Juan P. G.. Universidad Autónoma de Madrid; España
Fil: Levin, Mariano Jorge. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Tellez, Maria Teresa. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina
description Trypanosoma cruzi ribosomes from epimastigote forms were purified as determined by electron microscopy and isoelectrofocusing was used to analyse this purified ribosome fraction. Silver stained gels revealed that acidic proteins are present in at least 10 different isoforms, in accord with previous cloning studies. To detect phosphorylation, in vitro phosphorylation assays using the recombinant protein TcP2β-mbp were carried out. The results showed that T. cruzi cytosolic fraction possesses protein kinase activity able to phosphorylate the recombinant protein. Purified ribosomes contain protein kinases that could also phosphorylate the recombinant protein TcP2β-mbp. Labelling parasites with [32Pi] in a phosphate free medium demonstrated that ribosome proteins, recognised with a specific mouse antiserum against recombinant TcP2β proteins, are phosphorylated in vivo. All these results suggest that in vivo phosphorylation of ribosome TcP2β proteins are mediated by protein kinase(s) not yet identified.
publishDate 2001
dc.date.none.fl_str_mv 2001-12
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/11336/79331
Gomez, Eliana B.; Medina, Gabriel; Ballesta, Juan P. G.; Levin, Mariano Jorge; Tellez, Maria Teresa; Acidic ribosomal P proteins are phosphorylated in Trypanosoma cruzi; Elsevier; International Journal for Parasitology; 31; 10; 12-2001; 1032-1039
0020-7519
CONICET Digital
CONICET
url http://hdl.handle.net/11336/79331
identifier_str_mv Gomez, Eliana B.; Medina, Gabriel; Ballesta, Juan P. G.; Levin, Mariano Jorge; Tellez, Maria Teresa; Acidic ribosomal P proteins are phosphorylated in Trypanosoma cruzi; Elsevier; International Journal for Parasitology; 31; 10; 12-2001; 1032-1039
0020-7519
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0020751901002193
info:eu-repo/semantics/altIdentifier/doi/10.1016/S0020-7519(01)00219-3
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.22299

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