Publication:
Ribosomal protein eL39 is important for maturation of the nascent polypeptide exit tunnel and proper protein folding during translation.

dc.contributor.authorMicic, Jelena
dc.contributor.authorRodriguez-Galan, Olga
dc.contributor.authorBabiano, Reyes
dc.contributor.authorFitzgerald, Fiona
dc.contributor.authorFernandez-Fernandez, Jose
dc.contributor.authorZhang, Yunyang
dc.contributor.authorGao, Ning
dc.contributor.authorWoolford, John L
dc.contributor.authorde-la-Cruz, Jesus
dc.date.accessioned2023-05-03T13:27:43Z
dc.date.available2023-05-03T13:27:43Z
dc.date.issued2022
dc.description.abstractDuring 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.
dc.description.versionSi
dc.identifier.citationMicic J, Rodríguez-Galán O, Babiano R, Fitzgerald F, Fernández-Fernández J, Zhang Y, et al. Ribosomal protein eL39 is important for maturation of the nascent polypeptide exit tunnel and proper protein folding during translation. Nucleic Acids Res. 2022 Jun 24;50(11):6453-6473.
dc.identifier.doi10.1093/nar/gkac366
dc.identifier.essn1362-4962
dc.identifier.pmcPMC9226512
dc.identifier.pmid35639884
dc.identifier.pubmedURLhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC9226512/pdf
dc.identifier.unpaywallURLhttps://academic.oup.com/nar/article-pdf/50/11/6453/44144917/gkac366.pdf
dc.identifier.urihttp://hdl.handle.net/10668/19814
dc.issue.number11
dc.journal.titleNucleic acids research
dc.journal.titleabbreviationNucleic Acids Res
dc.language.isoen
dc.organizationHospital Universitario Virgen del Rocío
dc.organizationInstituto de Biomedicina de Sevilla-IBIS
dc.page.number6453-6473
dc.provenanceRealizada la curación de contenido 08/07/2025.
dc.publisherOxford University Press
dc.pubmedtypeJournal Article
dc.pubmedtypeResearch Support, N.I.H., Extramural
dc.pubmedtypeResearch Support, Non-U.S. Gov't
dc.relation.publisherversionhttps://academic.oup.com/nar/article-lookup/doi/10.1093/nar/gkac366
dc.rightsAttribution 4.0 International
dc.rights.accessRightsopen access
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.subjectRibosome assembly
dc.subjectNascent polypeptide exit tunnel
dc.subjectRibosomal protein uL4
dc.subjectRibosomal protein uL22
dc.subjectRibosomal protein eL39
dc.subject60S ribosomal subunit
dc.subject.meshCryoelectron Microscopy
dc.subject.meshModels, Molecular
dc.subject.meshPeptides
dc.subject.meshProtein Folding
dc.subject.meshRNA, Ribosomal
dc.subject.meshRibosomal Proteins
dc.subject.meshRibosome Subunits, Large, Eukaryotic
dc.subject.meshSaccharomyces cerevisiae
dc.subject.meshSaccharomyces cerevisiae Proteins
dc.subject.meshEnsamblaje de ribosomas
dc.subject.meshRibosomal Subunits, Large
dc.subject.meshRibosomal Proteins
dc.subject.mesh60S Ribosomal Subunit
dc.subject.meshRNA, Ribosomal
dc.subject.meshPeptide Chain Elongation
dc.titleRibosomal protein eL39 is important for maturation of the nascent polypeptide exit tunnel and proper protein folding during translation.
dc.typeresearch article
dc.type.hasVersionVoR
dc.volume.number50
dspace.entity.typePublication

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