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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/79331
Ver los metadatos del registro completo
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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 Técnicas2025-09-29T10:09:27Zoai: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:34982025-09-29 10:09:27.699CONICET 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 |
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CONICET Digital (CONICET) |
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CONICET Digital (CONICET) |
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Consejo Nacional de Investigaciones Científicas y Técnicas |
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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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13.070432 |