Repository logo
 
Publication

A role for DIS3L2 over natural nonsense-mediated mRNA decay targets in human cells

2019-10-22Journal article Restricted access
Simple item page
dc.contributor.authorCosta, Paulo J. da
dc.contributor.authorMenezes, Juliane
dc.contributor.authorSaramago, Margarida
dc.contributor.authorGarcía-Moreno, Juan F.
dc.contributor.authorSantos, Hugo A.
dc.contributor.authorGama-Carvalho, Margarida
dc.contributor.authorArraiano, Cecília M.
dc.contributor.authorRomão, Luísa
dc.date.accessioned2020-04-20T19:48:20Z
dc.date.available2020-10-22T00:30:13Z
dc.date.issued2019-10-22
dc.descriptionSupplementary data to this article can be found online at https://doi.org/10.1016/j.bbrc.2019.08.105.pt_PT
dc.description.abstractThe nonsense-mediated decay (NMD) pathway selectively degrades mRNAs carrying a premature translation-termination codon but also regulates the abundance of a large number of physiological mRNAs that encode full-length proteins. In human cells, NMD-targeted mRNAs are degraded by endonucleolytic cleavage and exonucleolytic degradation from both 5-' and 3'-ends. This is done by a process not yet completely understood that recruits decapping and 5'-to-3' exonuclease activities, as well as deadenylating and 3'-to-5' exonuclease exosome activities. In yeast, DIS3/Rrp44 protein is the catalytic subunit of the exosome, but in humans, there are three known paralogues of this enzyme: DIS3, DIS3L1, and DIS3L2. However, little is known about their role in NMD. Here, we show that some NMD-targets are DIS3L2 substrates in human cells. In addition, we observed that DIS3L2 acts over full-length transcripts, through a process that also involves UPF1. Moreover, DIS3L2-mediated decay is dependent on the activity of the terminal uridylyl transferases Zcchc6/11 (TUT7/4). Together, our findings establish a role for DIS3L2 and uridylation in NMD.pt_PT
dc.description.abstractHighlights: DIS3L2 functions in the decay of natural NMD-targets in a transcript-specific manner; DIS3L2 acts over full-length NMD-targets, through a process that also involves UPF1; DIS3L2 function in NMD is dependent on the terminal uridylyl transferases Zcchc6/11.pt_PT
dc.description.sponsorshipThis work was partially supported by Fundaçao para a Ci ~ encia e ^ a Tecnologia (FCT) (PTFC/BIM-MEC/3749/2014 to LR and UID/ MULTI/04046/2013 to BioISI). PJdC, HAS and JFG-M are recipients of a fellowship from BioSys PhD programme (SFRH/BD/52495/2014, SFRH/BD/52492/2014, and PD/BD/142898/2018, respectively) and JM is a posdoc fellow (SFRH/BPD/98360/2013) from FCT. Work at ITQB-NOVA was financially supported by: Project LISBOA-01-0145-FEDER-007660 funded by the European Regional Development Fund (FEDER) through COMPETE2020 - Programa Operacional Competitividade e Internacionalizaçao (POCI) and by FCT funds: ~ PTDC/BIA-MIC/1399/2014 to CMA and PTDC/BIM-MEC/3749/2014 to SCV. SCV was financed by program IF of FCT (IF/00217/2015). MS was financed by an FCT contract according to DL57/2016 [SFRH/ BPD/109464/2015]. We thank Dr. V. Narry Kim from Seoul National University, who kindly provided us with the pCK-FLAG-TUT4 and pCK-FLAG-TUT7 vectors.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationBiochem Biophys Res Commun. 2019 Oct 22;518(4):664-671. doi: 10.1016/j.bbrc.2019.08.105. Epub 2019 Aug 26.pt_PT
dc.identifier.doi10.1016/j.bbrc.2019.08.105pt_PT
dc.identifier.issn0006-291X
dc.identifier.urihttp://hdl.handle.net/10400.18/6466
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherElsevier/ Academic Presspt_PT
dc.relation.publisherversionhttps://www.sciencedirect.com/science/article/pii/S0006291X19316286?via%3Dihubpt_PT
dc.subjectNonsense-mediated mRNA Decaypt_PT
dc.subjectNMDpt_PT
dc.subjectDIS3L2pt_PT
dc.subjectTerminal Uridylyl Transferases Zcchc6/11pt_PT
dc.subjectTUT7/4pt_PT
dc.subjectmRNA Turnoverpt_PT
dc.subjectDoenças Genéticaspt_PT
dc.subjectGenómica Funcional e Estruturalpt_PT
dc.titleA role for DIS3L2 over natural nonsense-mediated mRNA decay targets in human cellspt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/5876/UID%2FMulti%2F04046%2F2013/PT
oaire.citation.endPage671pt_PT
oaire.citation.issue4pt_PT
oaire.citation.startPage664pt_PT
oaire.citation.titleBiochemical and Biophysical Research Communicationspt_PT
oaire.citation.volume518pt_PT
oaire.fundingStream5876
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.embargofctDe acordo com política editorial da revista.pt_PT
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
relation.isProjectOfPublicationdc84f768-e6f2-4eea-b294-6c8ebbd1a156
relation.isProjectOfPublication.latestForDiscoverydc84f768-e6f2-4eea-b294-6c8ebbd1a156

Files

Original bundle
Now showing 1 - 1 of 1
No Thumbnail Available
Name:
da Costa et al._1.pdf
Size:
1.88 MB
Format:
Adobe Portable Document Format
Download
License bundle
Now showing 1 - 1 of 1
No Thumbnail Available
Name:
license.txt
Size:
1.71 KB
Format:
Item-specific license agreed upon to submission
Description:
Download

Collections

DGH - Artigos em revistas internacionais