dc.creator | Micic, Jelena | es |
dc.creator | Rodríguez Galán, Olga | es |
dc.creator | Babiano González, Reyes | es |
dc.creator | Fitzgerald, Fiona | es |
dc.creator | Fernández Fernández, José | es |
dc.creator | Gao, Ning | es |
dc.creator | Woolford, John L. | es |
dc.creator | Cruz Díaz, Jesús de la | es |
dc.date.accessioned | 2022-07-11T08:36:19Z | |
dc.date.available | 2022-07-11T08:36:19Z | |
dc.date.issued | 2022 | |
dc.identifier.citation | Micic, J., Rodríguez Galán, O., Babiano González, R., Fitzgerald, F., Fernández Fernández, J., Gao, N.,...,Cruz Díaz, J.d.l. (2022). Ribosomal protein eL39 is important for maturation of the nascent polypeptide exit tunnel and proper protein folding during translation. Nucleic Acids Research, 50 (11), 6453-6473. | |
dc.identifier.issn | 1362-4962 | es |
dc.identifier.uri | https://hdl.handle.net/11441/135192 | |
dc.description.abstract | During translation, nascent polypeptide chains travel
from the peptidyl transferase center through the
nascent polypeptide exit tunnel (NPET) to emerge
from 60S subunits. The NPET includes portions of
five of the six 25S/5.8S rRNA domains and ribosomal proteins uL4, uL22, and eL39. Internal loops
of uL4 and uL22 form the constriction sites of the
NPET and are important for both assembly and function of ribosomes. Here, we investigated the roles
of eL39 in tunnel construction, 60S biogenesis, and
protein synthesis. We show that eL39 is important for
proper protein folding during translation. Consistent
with a delay in processing of 27S and 7S pre-rRNAs,
eL39 functions in pre-60S assembly during middle
nucleolar stages. Our biochemical assays suggest
the presence of eL39 in particles at these stages, although it is not visualized in them by cryo-electron
microscopy. This indicates that eL39 takes part in
assembly even when it is not fully accommodated
into the body of pre-60S particles. eL39 is also important for later steps of assembly, rotation of the 5S
ribonucleoprotein complex, likely through long range
rRNA interactions. Finally, our data strongly suggest
the presence of alternative pathways of ribosome
assembly, previously observed in the biogenesis of
bacterial ribosomal subunits. | es |
dc.description.sponsorship | España, Junta de Andalucía P20 00581, BIO-271 | es |
dc.description.sponsorship | España MCIN BES-2017-080876 | es |
dc.description.sponsorship | USA National Institutes of Health R01GM028301 | es |
dc.format | application/pdf | es |
dc.format.extent | 21 p. | es |
dc.language.iso | eng | es |
dc.publisher | Oxford University Press | es |
dc.relation.ispartof | Nucleic Acids Research, 50 (11), 6453-6473. | |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.title | Ribosomal protein eL39 is important for maturation of the nascent polypeptide exit tunnel and proper protein folding during translation | 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.projectID | P20 00581, BIO-271 | es |
dc.relation.projectID | BES-2017-080876 | es |
dc.relation.projectID | R01GM028301 | es |
dc.relation.publisherversion | https://dx.doi.org/10.1093/nar/gkac366 | es |
dc.identifier.doi | 10.1093/nar/gkac366 | es |
dc.journaltitle | Nucleic Acids Research | es |
dc.publication.volumen | 50 | es |
dc.publication.issue | 11 | es |
dc.publication.initialPage | 6453 | es |
dc.publication.endPage | 6473 | es |
dc.contributor.funder | Junta de Andalucía | es |
dc.contributor.funder | Ministerio de Ciencia e Innovación (MICIN). España | es |
dc.contributor.funder | National Institutes of Health. United States | es |