Proteomic analysis of the Trypanosoma cruzi ribosomal proteins
- Autores
- Juri Ayub, Maximiliano; Atwood, James; Nuccio, Arthur; Tarleton, Rick; Levin, Mariano Jorge
- Año de publicación
- 2009
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Trypanosoma cruzi is a parasite responsible for Chagas disease. The identification of new targets for chemotherapy is a major challenge for the control of this disease. Several lines of evidences suggest that the translational system in trypanosomatids show important differences compared to other eukaryotes. However, there little is known information about this. We have performed a detailed data mining search for ribosomal protein genes in T. cruzi genome data base combined with mass spectrometry analysis of purified T. cruzi ribosomes. Our results show that T. cruzi ribosomal proteins have ∼50% sequence identity to yeast ones. Nevertheless, some parasite proteins are longer due to the presence of several N- or C-terminal extensions, which are exclusive of trypanosomatids. In particular, L19 and S21 show C-terminal extensions of 168 and 164 amino acids, respectively. In addition, we detected two 60S subunit proteins that had not been previously detected in the T. cruzi total proteome; namely, L22 and L42.
Fil: Juri Ayub, Maximiliano. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis. Universidad Nacional de San Luis. Facultad de Ciencias Físico Matemáticas y Naturales. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; Argentina
Fil: Atwood, James. Georgia State University; Estados Unidos
Fil: Nuccio, Arthur. Georgia State University; Estados Unidos
Fil: Tarleton, Rick. Georgia State University; Estados Unidos
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 - Materia
-
MASS SPECTROMETRY
PROTEIN SYNTHESIS
RIBOSOME
TRYPANOSOMA CRUZI - 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:11336/130750
Ver los metadatos del registro completo
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Proteomic analysis of the Trypanosoma cruzi ribosomal proteinsJuri Ayub, MaximilianoAtwood, JamesNuccio, ArthurTarleton, RickLevin, Mariano JorgeMASS SPECTROMETRYPROTEIN SYNTHESISRIBOSOMETRYPANOSOMA CRUZIhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Trypanosoma cruzi is a parasite responsible for Chagas disease. The identification of new targets for chemotherapy is a major challenge for the control of this disease. Several lines of evidences suggest that the translational system in trypanosomatids show important differences compared to other eukaryotes. However, there little is known information about this. We have performed a detailed data mining search for ribosomal protein genes in T. cruzi genome data base combined with mass spectrometry analysis of purified T. cruzi ribosomes. Our results show that T. cruzi ribosomal proteins have ∼50% sequence identity to yeast ones. Nevertheless, some parasite proteins are longer due to the presence of several N- or C-terminal extensions, which are exclusive of trypanosomatids. In particular, L19 and S21 show C-terminal extensions of 168 and 164 amino acids, respectively. In addition, we detected two 60S subunit proteins that had not been previously detected in the T. cruzi total proteome; namely, L22 and L42.Fil: Juri Ayub, Maximiliano. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis. Universidad Nacional de San Luis. Facultad de Ciencias Físico Matemáticas y Naturales. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; ArgentinaFil: Atwood, James. Georgia State University; Estados UnidosFil: Nuccio, Arthur. Georgia State University; Estados UnidosFil: Tarleton, Rick. Georgia State University; Estados UnidosFil: Levin, Mariano Jorge. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; ArgentinaAcademic Press Inc Elsevier Science2009-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/130750Juri Ayub, Maximiliano; Atwood, James; Nuccio, Arthur; Tarleton, Rick; Levin, Mariano Jorge; Proteomic analysis of the Trypanosoma cruzi ribosomal proteins; Academic Press Inc Elsevier Science; Biochemical and Biophysical Research Communications; 382; 1; 2-2009; 30-340006-291XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S0006291X0900360Xinfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbrc.2009.02.095info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:45:36Zoai:ri.conicet.gov.ar:11336/130750instacron: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 15:45:36.477CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Proteomic analysis of the Trypanosoma cruzi ribosomal proteins |
title |
Proteomic analysis of the Trypanosoma cruzi ribosomal proteins |
spellingShingle |
Proteomic analysis of the Trypanosoma cruzi ribosomal proteins Juri Ayub, Maximiliano MASS SPECTROMETRY PROTEIN SYNTHESIS RIBOSOME TRYPANOSOMA CRUZI |
title_short |
Proteomic analysis of the Trypanosoma cruzi ribosomal proteins |
title_full |
Proteomic analysis of the Trypanosoma cruzi ribosomal proteins |
title_fullStr |
Proteomic analysis of the Trypanosoma cruzi ribosomal proteins |
title_full_unstemmed |
Proteomic analysis of the Trypanosoma cruzi ribosomal proteins |
title_sort |
Proteomic analysis of the Trypanosoma cruzi ribosomal proteins |
dc.creator.none.fl_str_mv |
Juri Ayub, Maximiliano Atwood, James Nuccio, Arthur Tarleton, Rick Levin, Mariano Jorge |
author |
Juri Ayub, Maximiliano |
author_facet |
Juri Ayub, Maximiliano Atwood, James Nuccio, Arthur Tarleton, Rick Levin, Mariano Jorge |
author_role |
author |
author2 |
Atwood, James Nuccio, Arthur Tarleton, Rick Levin, Mariano Jorge |
author2_role |
author author author author |
dc.subject.none.fl_str_mv |
MASS SPECTROMETRY PROTEIN SYNTHESIS RIBOSOME TRYPANOSOMA CRUZI |
topic |
MASS SPECTROMETRY PROTEIN SYNTHESIS RIBOSOME TRYPANOSOMA CRUZI |
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 is a parasite responsible for Chagas disease. The identification of new targets for chemotherapy is a major challenge for the control of this disease. Several lines of evidences suggest that the translational system in trypanosomatids show important differences compared to other eukaryotes. However, there little is known information about this. We have performed a detailed data mining search for ribosomal protein genes in T. cruzi genome data base combined with mass spectrometry analysis of purified T. cruzi ribosomes. Our results show that T. cruzi ribosomal proteins have ∼50% sequence identity to yeast ones. Nevertheless, some parasite proteins are longer due to the presence of several N- or C-terminal extensions, which are exclusive of trypanosomatids. In particular, L19 and S21 show C-terminal extensions of 168 and 164 amino acids, respectively. In addition, we detected two 60S subunit proteins that had not been previously detected in the T. cruzi total proteome; namely, L22 and L42. Fil: Juri Ayub, Maximiliano. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis. Universidad Nacional de San Luis. Facultad de Ciencias Físico Matemáticas y Naturales. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; Argentina Fil: Atwood, James. Georgia State University; Estados Unidos Fil: Nuccio, Arthur. Georgia State University; Estados Unidos Fil: Tarleton, Rick. Georgia State University; Estados Unidos 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 |
description |
Trypanosoma cruzi is a parasite responsible for Chagas disease. The identification of new targets for chemotherapy is a major challenge for the control of this disease. Several lines of evidences suggest that the translational system in trypanosomatids show important differences compared to other eukaryotes. However, there little is known information about this. We have performed a detailed data mining search for ribosomal protein genes in T. cruzi genome data base combined with mass spectrometry analysis of purified T. cruzi ribosomes. Our results show that T. cruzi ribosomal proteins have ∼50% sequence identity to yeast ones. Nevertheless, some parasite proteins are longer due to the presence of several N- or C-terminal extensions, which are exclusive of trypanosomatids. In particular, L19 and S21 show C-terminal extensions of 168 and 164 amino acids, respectively. In addition, we detected two 60S subunit proteins that had not been previously detected in the T. cruzi total proteome; namely, L22 and L42. |
publishDate |
2009 |
dc.date.none.fl_str_mv |
2009-02 |
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/11336/130750 Juri Ayub, Maximiliano; Atwood, James; Nuccio, Arthur; Tarleton, Rick; Levin, Mariano Jorge; Proteomic analysis of the Trypanosoma cruzi ribosomal proteins; Academic Press Inc Elsevier Science; Biochemical and Biophysical Research Communications; 382; 1; 2-2009; 30-34 0006-291X CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/130750 |
identifier_str_mv |
Juri Ayub, Maximiliano; Atwood, James; Nuccio, Arthur; Tarleton, Rick; Levin, Mariano Jorge; Proteomic analysis of the Trypanosoma cruzi ribosomal proteins; Academic Press Inc Elsevier Science; Biochemical and Biophysical Research Communications; 382; 1; 2-2009; 30-34 0006-291X 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/abs/pii/S0006291X0900360X info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbrc.2009.02.095 |
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 application/pdf |
dc.publisher.none.fl_str_mv |
Academic Press Inc Elsevier Science |
publisher.none.fl_str_mv |
Academic Press Inc Elsevier Science |
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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13.22299 |