dc.creator | Pillet, Benjamin | es |
dc.creator | García Gómez, Juan José | es |
dc.creator | Pausch, Patrick | es |
dc.creator | Falquet, Laurent | es |
dc.creator | Bange, Gert | es |
dc.creator | Cruz Díaz, Jesús de la | es |
dc.creator | Kressler, Dieter | es |
dc.date.accessioned | 2016-08-08T11:07:44Z | |
dc.date.available | 2016-08-08T11:07:44Z | |
dc.date.issued | 2015 | |
dc.identifier.citation | Pillet, B., García Gómez, J.J., Pausch, P., Falquet, L., Bange, G., Cruz Díaz, J.d.l. y Kressler, D. (2015). The dedicated chaperone acl4 escorts ribosomal protein rpl4 to its nuclear pre-60s assembly site. PLoS Genetics, 11 (10), 1-34. | |
dc.identifier.issn | 1553-7390 | es |
dc.identifier.uri | http://hdl.handle.net/11441/44288 | |
dc.description.abstract | Ribosomes are the highly complex macromolecular assemblies dedicated to the synthesis
of all cellular proteins from mRNA templates. The main principles underlying the making of
ribosomes are conserved across eukaryotic organisms and this process has been studied
in most detail in the yeast Saccharomyces cerevisiae. Yeast ribosomes are composed of
four ribosomal RNAs (rRNAs) and 79 ribosomal proteins (r-proteins). Most r-proteins need
to be transported from the cytoplasm to the nucleus where they get incorporated into the
evolving pre-ribosomal particles. Due to the high abundance and difficult physicochemical
properties of r-proteins, their correct folding and fail-safe targeting to the assembly site
depends largely on general, as well as highly specialized, chaperone and transport systems. Many r-proteins contain universally conserved or eukaryote-specific internal loops
and/or terminal extensions, which were shown to mediate their nuclear targeting and association with dedicated chaperones in a growing number of cases. The 60S r-protein Rpl4 is
particularly interesting since it harbours a conserved long internal loop and a prominent Cterminal eukaryote-specific extension. Here we show that both the long internal loop and
the C-terminal eukaryote-specific extension are strictly required for the functionality of Rpl4.
While Rpl4 contains at least five distinct nuclear localization signals (NLS), the C-terminal
part of the long internal loop associates with a specific binding partner, termed Acl4.
Absence of Acl4 confers a severe slow-growth phenotype and a deficiency in the production
of 60S subunits. Genetic and biochemical evidence indicates that Acl4 can be considered
as a dedicated chaperone of Rpl4. Notably, Acl4 localizes to both the cytoplasm and
nucleus and it has the capacity to capture nascent Rpl4 in a co-translational manner. Taken
together, our findings indicate that the dedicated chaperone Acl4 accompanies Rpl4 from
the cytoplasm to its pre-60S assembly site in the nucleus | es |
dc.format | application/pdf | es |
dc.language.iso | eng | es |
dc.publisher | Public Library of Science | es |
dc.relation.ispartof | PLoS Genetics, 11 (10), 1-34. | |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.title | The dedicated chaperone acl4 escorts ribosomal protein rpl4 to its nuclear pre-60s assembly site | es |
dc.type | info:eu-repo/semantics/article | es |
dcterms.identifier | https://ror.org/03yxnpp24 | |
dc.type.version | info:eu-repo/semantics/publishedVersion | es |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | es |
dc.contributor.affiliation | Universidad de Sevilla. Departamento de Genética | es |
dc.relation.publisherversion | 10.1371/journal. pgen.1005565 | es |
dc.identifier.doi | 10.1371/journal. pgen.1005565 | es |
idus.format.extent | 35 p. | es |
dc.journaltitle | PLoS Genetics | es |
dc.publication.volumen | 11 | es |
dc.publication.issue | 10 | es |
dc.publication.initialPage | 1 | es |
dc.publication.endPage | 34 | es |
dc.identifier.idus | https://idus.us.es/xmlui/handle/11441/44288 | |