Show simple item record

dc.contributor.authorAlicante Martínez, Sara
dc.contributor.authorMuguruza Montero, Arantza
dc.contributor.authorBallesteros, Oscar R.
dc.contributor.authorMetola Martínez, Ane
dc.contributor.authorUrrutia Iñiguez, Janire
dc.contributor.authorVillarroel Muñoz, Álvaro
dc.contributor.authorNúñez Viadero, Eider ORCID
dc.date.accessioned2023-06-27T13:33:08Z
dc.date.available2023-06-27T13:33:08Z
dc.date.issued2023
dc.identifier.citationEkaia 43 : 101-116 (2023)
dc.identifier.issn0214-9001
dc.identifier.urihttp://hdl.handle.net/10810/61660
dc.description.abstractProteins are synthesised as linear polymers and must fold into their native three-dimensional structure to perform various functions in the cell. Understanding protein folding is crucial because protein misfolding is at the origin of several neurodegenerative diseases. Protein folding can start cotranslationally, i.e. when the emerging peptide is still asso-ciated with the ribosome. Indeed, it has been shown that more than one third of the cell’s proteins fold in the limited space of the ribosome tunnel. Increasing evidence suggests that the ribosome plays a critical role in protein folding. The ribosome can facilitate protein compaction, cause the creation of non-visible media in solution or delay the onset of folding. However, the study of cotranslational folding presents serious difficulties, mainly due to the limitations of the different current techniques. Hence, most studies on protein folding are based on proteins in solution, which are carried out by unfolding and refolding the protein, without taking into account the role of the ribosome in this process. In this article, we summarised the techniques developed in recent years for the study of cotranslational protein folding.; Proteinak polimero lineal gisa sintetizatzen dira eta beren jatorrizko egitura tridimentsionalean tolestu behar dira zelulan hainbat funtzio betetzeko. Proteinen tolespena ulertzea funtsezkoa da, tolespen okerrak hainbat gaixotasun neuro-degeneratiboren jatorria direlako. Proteinen tolespena modu koitzultzailean has daiteke, hau da, sortzen ari den peptidoa erribosomari lotuta dagoenean oraindik. Izan ere, zelularen proteinen heren bat baino gehiago erribosomaren tunelaren espazio mugatuan tolesten direla frogatu da, hau da, erribosomaren gainazalarekiko interakzioek modulatuta eta erribosoma-tunelaren beraren mugen pean. Gero eta ebidentzia gehiagok iradokitzen dute erribosomak funtsezko zeregina duela proteinen tolespenean. Erribosomak proteina trinkotzea erraztu dezake, soluzioan ikusten ez diren bitartekoak sortzea eragin dezake edo tolestearen hasiera atzeratu dezake. Hala ere, proteinen koitzulpenezko tolesdura aztertzeak zailtasun handiak ditu, batik bat, egungo teknikek dituzten mugengatik. Hori dela eta, proteinen tolesteari buruzko ikerketa gehienak soluzioan dauden proteinetan oinarritzen dira, proteina tolestuz eta destolestuz egiten direnak, prozesu horretan erribosomak duen rola kontuan hartu gabe. Artikulu honetan, azken urteotan proteinen koitzulpenezko tolestura ikertzeko garatu diren tekniken laburpena egin da.
dc.language.isoeus
dc.publisherServicio Editorial de la Universidad del País Vasco/Euskal Herriko Unibertsitatearen Argitalpen Zerbitzua
dc.rightsinfo:eu-repo/semantics/openAccess
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/
dc.titleProteinen tolestura tunel erribosomikoan
dc.typeinfo:eu-repo/semantics/article
dc.rights.holder© 2023 UPV/EHU Attribution-NonCommercial-ShareAlike 4.0 International
dc.identifier.doi10.1387/ekaia.23624


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record

© 2023 UPV/EHU Attribution-NonCommercial-ShareAlike 4.0 International
Except where otherwise noted, this item's license is described as © 2023 UPV/EHU Attribution-NonCommercial-ShareAlike 4.0 International