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dc.contributor.authorJamar, Nur Hidayah
dc.contributor.authorKritsiligkou, Paraskevi; orcid: 0000-0003-2452-141X
dc.contributor.authorGrant, Chris M.; orcid: 0000-0002-0616-6576; email: chris.grant@manchester.ac.uk
dc.date.accessioned2021-08-11T15:49:51Z
dc.date.available2021-08-11T15:49:51Z
dc.date.issued2018-03-01
dc.date.submitted2017-12-04
dc.identifierhttps://chesterrep.openrepository.com/bitstream/handle/10034/625548/41598_2018_Article_22183.pdf?sequence=2
dc.identifierhttps://chesterrep.openrepository.com/bitstream/handle/10034/625548/additional-files.zip?sequence=3
dc.identifierhttps://chesterrep.openrepository.com/bitstream/handle/10034/625548/41598_2018_Article_22183_nlm.xml?sequence=4
dc.identifierhttps://chesterrep.openrepository.com/bitstream/handle/10034/625548/41598_2018_22183_MOESM1_ESM.pdf?sequence=5
dc.identifier.citationScientific Reports, volume 8, issue 1, page 3894
dc.identifier.urihttp://hdl.handle.net/10034/625548
dc.descriptionFrom Springer Nature via Jisc Publications Router
dc.descriptionHistory: received 2017-12-04, accepted 2018-02-15, registration 2018-02-19, pub-electronic 2018-03-01, online 2018-03-01, collection 2018-12
dc.descriptionPublication status: Published
dc.description.abstractAbstract: Eukaryotic cells contain translation-associated mRNA surveillance pathways which prevent the production of potentially toxic proteins from aberrant mRNA translation events. We found that loss of mRNA surveillance pathways in mutants deficient in nonsense-mediated decay (NMD), no-go decay (NGD) and nonstop decay (NSD) results in increased protein aggregation. We have isolated and identified the proteins that aggregate and our bioinformatic analyses indicates that increased aggregation of aggregation-prone proteins is a general occurrence in mRNA surveillance mutants, rather than being attributable to specific pathways. The proteins that aggregate in mRNA surveillance mutants tend to be more highly expressed, more abundant and more stable proteins compared with the wider proteome. There is also a strong correlation with the proteins that aggregate in response to nascent protein misfolding and an enrichment for proteins that are substrates of ribosome-associated Hsp70 chaperones, consistent with susceptibility for aggregation primarily occurring during translation/folding. We also identified a significant overlap between the aggregated proteins in mRNA surveillance mutants and ageing yeast cells suggesting that translation-dependent protein aggregation may be a feature of the loss of proteostasis that occurs in aged cell populations.
dc.languageen
dc.publisherNature Publishing Group UK
dc.rightsLicence for this article: http://creativecommons.org/licenses/by/4.0/
dc.sourceeissn: 2045-2322
dc.subjectArticle
dc.subject/631/45/470/1981
dc.subject/631/45/470/2284
dc.subject/631/337/574
dc.subject/82
dc.subject/82/58
dc.subjectarticle
dc.titleLoss of mRNA surveillance pathways results in widespread protein aggregation
dc.typearticle
dc.date.updated2021-08-11T15:49:50Z
dc.date.accepted2018-02-15


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