Convergent evolution led ribosome inactivating proteins to interact with ribosomal stalk
- Autores
- Lapadula, Walter Jesús; Sanchez Puerta, Maria Virginia; Juri Ayub, Maximiliano
- Año de publicación
- 2012
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Ribosome-inactivating proteins (RIPs) inhibit protein synthesis by depurinating an adenine on the sarcin–ricin loop (SRL) of the large subunit ribosomal RNA. Several RIPs interact with the C-terminal end of ribosomal stalk P proteins, and this interaction is required for their full activity. In contrast, the activity of Pokeweed Antiviral Protein is not affected by blocking this stalk component. Here, we provide evidence from phylogenetic analyses and sequence alignments suggesting that the interaction with the C-terminal end of P proteins evolved independently in different RIPs by convergent evolution.
Fil: Lapadula, Walter Jesús. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Bioquímica y Ciencias Biológicas. Area de Biología Molecular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; Argentina
Fil: Sanchez Puerta, Maria Virginia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mendoza. Instituto de Biología Agrícola de Mendoza; Argentina. Universidad Nacional de Cuyo; Argentina
Fil: Juri Ayub, Maximiliano. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; Argentina. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Bioquímica y Ciencias Biológicas. Area de Biología Molecular; Argentina - Materia
-
Ribosome Inactivating Proteins
Stalk
Phylogeny - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/14500
Ver los metadatos del registro completo
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Convergent evolution led ribosome inactivating proteins to interact with ribosomal stalkLapadula, Walter JesúsSanchez Puerta, Maria VirginiaJuri Ayub, MaximilianoRibosome Inactivating ProteinsStalkPhylogenyhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Ribosome-inactivating proteins (RIPs) inhibit protein synthesis by depurinating an adenine on the sarcin–ricin loop (SRL) of the large subunit ribosomal RNA. Several RIPs interact with the C-terminal end of ribosomal stalk P proteins, and this interaction is required for their full activity. In contrast, the activity of Pokeweed Antiviral Protein is not affected by blocking this stalk component. Here, we provide evidence from phylogenetic analyses and sequence alignments suggesting that the interaction with the C-terminal end of P proteins evolved independently in different RIPs by convergent evolution.Fil: Lapadula, Walter Jesús. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Bioquímica y Ciencias Biológicas. Area de Biología Molecular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; ArgentinaFil: Sanchez Puerta, Maria Virginia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mendoza. Instituto de Biología Agrícola de Mendoza; Argentina. Universidad Nacional de Cuyo; ArgentinaFil: Juri Ayub, Maximiliano. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; Argentina. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Bioquímica y Ciencias Biológicas. Area de Biología Molecular; ArgentinaElsevier2012-01info: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/11336/14500Lapadula, Walter Jesús; Sanchez Puerta, Maria Virginia; Juri Ayub, Maximiliano; Convergent evolution led ribosome inactivating proteins to interact with ribosomal stalk; Elsevier; Toxicon; 59; 3; 1-2012; 427-4320041-0101enginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0041010112000025info:eu-repo/semantics/altIdentifier/doi/10.1016/j.toxicon.2011.12.014info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:44:45Zoai:ri.conicet.gov.ar:11336/14500instacron: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:34982025-09-03 09:44:45.381CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Convergent evolution led ribosome inactivating proteins to interact with ribosomal stalk |
title |
Convergent evolution led ribosome inactivating proteins to interact with ribosomal stalk |
spellingShingle |
Convergent evolution led ribosome inactivating proteins to interact with ribosomal stalk Lapadula, Walter Jesús Ribosome Inactivating Proteins Stalk Phylogeny |
title_short |
Convergent evolution led ribosome inactivating proteins to interact with ribosomal stalk |
title_full |
Convergent evolution led ribosome inactivating proteins to interact with ribosomal stalk |
title_fullStr |
Convergent evolution led ribosome inactivating proteins to interact with ribosomal stalk |
title_full_unstemmed |
Convergent evolution led ribosome inactivating proteins to interact with ribosomal stalk |
title_sort |
Convergent evolution led ribosome inactivating proteins to interact with ribosomal stalk |
dc.creator.none.fl_str_mv |
Lapadula, Walter Jesús Sanchez Puerta, Maria Virginia Juri Ayub, Maximiliano |
author |
Lapadula, Walter Jesús |
author_facet |
Lapadula, Walter Jesús Sanchez Puerta, Maria Virginia Juri Ayub, Maximiliano |
author_role |
author |
author2 |
Sanchez Puerta, Maria Virginia Juri Ayub, Maximiliano |
author2_role |
author author |
dc.subject.none.fl_str_mv |
Ribosome Inactivating Proteins Stalk Phylogeny |
topic |
Ribosome Inactivating Proteins Stalk Phylogeny |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Ribosome-inactivating proteins (RIPs) inhibit protein synthesis by depurinating an adenine on the sarcin–ricin loop (SRL) of the large subunit ribosomal RNA. Several RIPs interact with the C-terminal end of ribosomal stalk P proteins, and this interaction is required for their full activity. In contrast, the activity of Pokeweed Antiviral Protein is not affected by blocking this stalk component. Here, we provide evidence from phylogenetic analyses and sequence alignments suggesting that the interaction with the C-terminal end of P proteins evolved independently in different RIPs by convergent evolution. Fil: Lapadula, Walter Jesús. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Bioquímica y Ciencias Biológicas. Area de Biología Molecular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; Argentina Fil: Sanchez Puerta, Maria Virginia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mendoza. Instituto de Biología Agrícola de Mendoza; Argentina. Universidad Nacional de Cuyo; Argentina Fil: Juri Ayub, Maximiliano. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; Argentina. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Bioquímica y Ciencias Biológicas. Area de Biología Molecular; Argentina |
description |
Ribosome-inactivating proteins (RIPs) inhibit protein synthesis by depurinating an adenine on the sarcin–ricin loop (SRL) of the large subunit ribosomal RNA. Several RIPs interact with the C-terminal end of ribosomal stalk P proteins, and this interaction is required for their full activity. In contrast, the activity of Pokeweed Antiviral Protein is not affected by blocking this stalk component. Here, we provide evidence from phylogenetic analyses and sequence alignments suggesting that the interaction with the C-terminal end of P proteins evolved independently in different RIPs by convergent evolution. |
publishDate |
2012 |
dc.date.none.fl_str_mv |
2012-01 |
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/11336/14500 Lapadula, Walter Jesús; Sanchez Puerta, Maria Virginia; Juri Ayub, Maximiliano; Convergent evolution led ribosome inactivating proteins to interact with ribosomal stalk; Elsevier; Toxicon; 59; 3; 1-2012; 427-432 0041-0101 |
url |
http://hdl.handle.net/11336/14500 |
identifier_str_mv |
Lapadula, Walter Jesús; Sanchez Puerta, Maria Virginia; Juri Ayub, Maximiliano; Convergent evolution led ribosome inactivating proteins to interact with ribosomal stalk; Elsevier; Toxicon; 59; 3; 1-2012; 427-432 0041-0101 |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0041010112000025 info:eu-repo/semantics/altIdentifier/doi/10.1016/j.toxicon.2011.12.014 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-nd/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Elsevier |
publisher.none.fl_str_mv |
Elsevier |
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reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
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CONICET Digital (CONICET) |
collection |
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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13.13397 |