P1 and P2 protein heterodimer binding to the Po protein of Saccharomyces cerevisiae is relatively non-specific and a source of ribosomal heterogeneity

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License.

Detalhes bibliográficos
Autores: Cárdenas, David B., Revuelta-Cervantes, Jesús, Jiménez Díaz, Antonio, Camargo, Hendricka, Remacha, Miguel, Ballesta, Juan P. G.
Formato: artículo
Fecha de publicación:2012
País:España
Recursos:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/77570
Acesso em linha:http://hdl.handle.net/10261/77570
Access Level:acceso abierto
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spelling P1 and P2 protein heterodimer binding to the Po protein of Saccharomyces cerevisiae is relatively non-specific and a source of ribosomal heterogeneityCárdenas, David B.Revuelta-Cervantes, JesúsJiménez Díaz, AntonioCamargo, HendrickaRemacha, MiguelBallesta, Juan P. G.This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License.The ribosomal stalk is formed by four acidic phosphoproteins in Saccharomyces cerevisiae, P1α, P1β, P2α and P2β, which form two heterodimers, P1α/P2β and P1β/P2α, that preferentially bind to sites A and B of the P0 protein, respectively. Using mutant strains carrying only one of the four possible P1/P2 combinations, we found a specific phenotype associated to each P1/P2 pair, indicating that not all acidic P proteins play the same role. The absence of one P1/P2 heterodimer reduced the rate of cell growth by varying degrees, depending on the proteins missing. Synthesis of the 60S ribosomal subunit also decreased, particularly in strains carrying the unusual P1α-P2α or P1β-P2β heterodimers, although the distinct P1/P2 dimers are bound with similar affinity to the mutant ribosome. While in wild-type strains the B site bound P1β/P2α in a highly specific manner and the A site bound the four P proteins similarly, both the A and B binding sites efficiently bound practically any P1/P2 pair in mutant strains expressing truncated P0 proteins. The reported results support that while most ribosomes contain a P1α/P2β-P0- P1β/P2α structure in normal conditions, the stalk assembly mechanism can generate alternative compositions, which have been previously detected in the cell. © 2011 The Author(s).Spanish Ministry of Science and Innovation (MICINN) (grant BFU2009-09738 to J.P.G.B.); Fundación Ramón Areces (Institutional Grant to Centro de Biología Molecular Severo Ochoa). Funding for open access charge: Grant from the Spanish Ministry of Science and Innovation.Peer ReviewedOxford University PressMinisterio de Ciencia e Innovación (España)Fundación Ramón Areces2013201320122013info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501http://hdl.handle.net/10261/77570reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttp://dx.doi.org/10.1093/nar/gks036info:eu-repo/semantics/openAccessoai:digital.csic.es:10261/775702026-05-22T06:33:51Z
dc.title.none.fl_str_mv P1 and P2 protein heterodimer binding to the Po protein of Saccharomyces cerevisiae is relatively non-specific and a source of ribosomal heterogeneity
title P1 and P2 protein heterodimer binding to the Po protein of Saccharomyces cerevisiae is relatively non-specific and a source of ribosomal heterogeneity
spellingShingle P1 and P2 protein heterodimer binding to the Po protein of Saccharomyces cerevisiae is relatively non-specific and a source of ribosomal heterogeneity
Cárdenas, David B.
title_short P1 and P2 protein heterodimer binding to the Po protein of Saccharomyces cerevisiae is relatively non-specific and a source of ribosomal heterogeneity
title_full P1 and P2 protein heterodimer binding to the Po protein of Saccharomyces cerevisiae is relatively non-specific and a source of ribosomal heterogeneity
title_fullStr P1 and P2 protein heterodimer binding to the Po protein of Saccharomyces cerevisiae is relatively non-specific and a source of ribosomal heterogeneity
title_full_unstemmed P1 and P2 protein heterodimer binding to the Po protein of Saccharomyces cerevisiae is relatively non-specific and a source of ribosomal heterogeneity
title_sort P1 and P2 protein heterodimer binding to the Po protein of Saccharomyces cerevisiae is relatively non-specific and a source of ribosomal heterogeneity
dc.creator.none.fl_str_mv Cárdenas, David B.
Revuelta-Cervantes, Jesús
Jiménez Díaz, Antonio
Camargo, Hendricka
Remacha, Miguel
Ballesta, Juan P. G.
author Cárdenas, David B.
author_facet Cárdenas, David B.
Revuelta-Cervantes, Jesús
Jiménez Díaz, Antonio
Camargo, Hendricka
Remacha, Miguel
Ballesta, Juan P. G.
author_role author
author2 Revuelta-Cervantes, Jesús
Jiménez Díaz, Antonio
Camargo, Hendricka
Remacha, Miguel
Ballesta, Juan P. G.
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Ministerio de Ciencia e Innovación (España)
Fundación Ramón Areces
description This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License.
publishDate 2012
dc.date.none.fl_str_mv 2012
2013
2013
2013
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/77570
url http://hdl.handle.net/10261/77570
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv http://dx.doi.org/10.1093/nar/gks036
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Oxford University Press
publisher.none.fl_str_mv Oxford University Press
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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