Document Detail


Protein N-terminal acetyltransferases act as N-terminal propionyltransferases in vitro and in vivo.
MedLine Citation:
PMID:  23043182     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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 (yNatAΔ) 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.
Authors:
Håvard Foyn; Petra Van Damme; Svein I Støve; Nina Glomnes; Rune Evjenth; Kris Gevaert; Thomas Arnesen
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2012-10-04
Journal Detail:
Title:  Molecular & cellular proteomics : MCP     Volume:  12     ISSN:  1535-9484     ISO Abbreviation:  Mol. Cell Proteomics     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2012-12-31     Completed Date:  2013-06-24     Revised Date:  2014-01-09    
Medline Journal Info:
Nlm Unique ID:  101125647     Medline TA:  Mol Cell Proteomics     Country:  United States    
Other Details:
Languages:  eng     Pagination:  42-54     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Acetyl Coenzyme A / metabolism
Acetylation
Acetyltransferases / genetics,  metabolism*
Amino Acids / metabolism
Cell Line
Humans
Lysine / metabolism
N-Terminal Acetyltransferases / genetics,  metabolism*
Protein Processing, Post-Translational
Proteome
Saccharomyces cerevisiae / genetics,  metabolism*
Saccharomyces cerevisiae Proteins / genetics,  metabolism*
Sequence Deletion
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Proteome; 0/Saccharomyces cerevisiae Proteins; 72-89-9/Acetyl Coenzyme A; EC 2.3.1.-/Acetyltransferases; EC 2.3.1.-/NatA protein, S cerevisiae; EC 2.3.1.88/N-Terminal Acetyltransferases; K3Z4F929H6/Lysine
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