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dc.contributor.authorGuzman, Ulises H.
dc.contributor.authorAksnes, Henriette
dc.contributor.authorRee, Rasmus
dc.contributor.authorKrogh, Nicolai
dc.contributor.authorJakobsson, Magnus
dc.contributor.authorJensen, Lars J.
dc.contributor.authorArnesen, Thomas
dc.contributor.authorOlsen, Jesper V.
dc.date.accessioned2023-10-09T08:19:46Z
dc.date.available2023-10-09T08:19:46Z
dc.date.created2023-10-02T12:38:58Z
dc.date.issued2023
dc.identifier.issn2041-1723
dc.identifier.urihttps://hdl.handle.net/11250/3095165
dc.description.abstractProtein N-terminal (Nt) acetylation is one of the most abundant modifications in eukaryotes, covering ~50-80 % of the proteome, depending on species. Cells with defective Nt-acetylation display a wide array of phenotypes such as impaired growth, mating defects and increased stress sensitivity. However, the pleiotropic nature of these effects has hampered our understanding of the functional impact of protein Nt-acetylation. The main enzyme responsible for Nt-acetylation throughout the eukaryotic kingdom is the N-terminal acetyltransferase NatA. Here we employ a multi-dimensional proteomics approach to analyze Saccharomyces cerevisiae lacking NatA activity, which causes global proteome remodeling. Pulsed-SILAC experiments reveals that NatA-deficient strains consistently increase degradation of ribosomal proteins compared to wild type. Explaining this phenomenon, thermal proteome profiling uncovers decreased thermostability of ribosomes in NatA-knockouts. Our data are in agreement with a role for Nt-acetylation in promoting stability for parts of the proteome by enhancing the avidity of protein-protein interactions and folding.en_US
dc.language.isoengen_US
dc.publisherNatureen_US
dc.rightsNavngivelse 4.0 Internasjonal*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/deed.no*
dc.titleLoss of N-terminal acetyltransferase A activity induces thermally unstable ribosomal proteins and increases their turnover in Saccharomyces cerevisiaeen_US
dc.typeJournal articleen_US
dc.typePeer revieweden_US
dc.description.versionpublishedVersionen_US
dc.rights.holderCopyright 2023 The Author(s)en_US
dc.source.articlenumber4517en_US
cristin.ispublishedtrue
cristin.fulltextoriginal
cristin.qualitycode2
dc.identifier.doi10.1038/s41467-023-40224-x
dc.identifier.cristin2180912
dc.source.journalNature Communicationsen_US
dc.identifier.citationNature Communications. 2023, 14 (1), 4517.en_US
dc.source.volume14en_US
dc.source.issue1en_US


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