Matches in UGent Biblio for { <https://biblio.ugent.be/publication/3130694#aggregation> ?p ?o. }
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- aggregation classification "A1".
- aggregation creator B419930.
- aggregation creator B419931.
- aggregation creator B419932.
- aggregation creator B419933.
- aggregation creator B419934.
- aggregation creator person.
- aggregation creator person.
- aggregation date "2013".
- aggregation format "application/pdf".
- aggregation hasFormat 3130694.bibtex.
- aggregation hasFormat 3130694.csv.
- aggregation hasFormat 3130694.dc.
- aggregation hasFormat 3130694.didl.
- aggregation hasFormat 3130694.doc.
- aggregation hasFormat 3130694.json.
- aggregation hasFormat 3130694.mets.
- aggregation hasFormat 3130694.mods.
- aggregation hasFormat 3130694.rdf.
- aggregation hasFormat 3130694.ris.
- aggregation hasFormat 3130694.txt.
- aggregation hasFormat 3130694.xls.
- aggregation hasFormat 3130694.yaml.
- aggregation isPartOf urn:issn:1535-9476.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Biology and Life Sciences".
- aggregation title "Protein N-terminal acetyltransferases act as N-terminal propionyltransferases in vitro and in vivo".
- aggregation abstract "N-terminal acetylation (Nt-acetylation) is a highly abundant protein modification in eukaryotes catalyzed by N-terminal acetyltransferases (NATs), which transfer an acetyl group from acetyl coenzyme A to the alpha amino group of a nascent polypeptide. Nt-acetylation has emerged as an important protein modifier, steering protein degradation, protein complex formation and protein localization. Very recently, it was reported that some human proteins could carry a propionyl group at their N-terminus. Here, we investigated the generality of N-terminal propionylation by analyzing its proteome-wide occurrence in yeast and we identified 10 unique in vivo Nt-propionylated N-termini. Furthermore, by performing differential N-terminome analysis of a control yeast strain (yNatA), a yeast NatA deletion strain (yNatA Delta) or a yeast NatA deletion strain expressing human NatA (hNatA), we were able to demonstrate that in vivo Nt-propionylation of several proteins, displaying a NatA type substrate specificity profile, depended on the presence of either yeast or human NatA. Furthermore, in vitro Nt-propionylation assays using synthetic peptides, propionyl coenzyme A, and either purified human NATs or immunoprecipitated human NatA, clearly demonstrated that NATs are Nt-propionyltransferases (NPTs) per se. We here demonstrate for the first time that Nt-propionylation can occur in yeast and thus is an evolutionarily conserved process, and that the NATs are multifunctional enzymes acting as NPTs in vivo and in vitro, in addition to their main role as NATs, and their potential function as lysine acetyltransferases (KATs) and noncatalytic regulators.".
- aggregation authorList BK741542.
- aggregation endPage "54".
- aggregation issue "1".
- aggregation startPage "42".
- aggregation volume "12".
- aggregation aggregates 3130709.
- aggregation aggregates 3134573.
- aggregation isDescribedBy 3130694.
- aggregation similarTo mcp.M112.019299.
- aggregation similarTo LU-3130694.