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ProteomicsN-terminal acetylome analysis reveals an expanded substrate profile for the NatC N-terminal acetyltransferase complex in yeast
N-terminal acetylation is a conserved protein modification among eukaryotes, and the yeast Saccharomyces cerevisiae is a valuable model system for studying this modification. The enzymes responsible for the bulk of protein N-terminal acetylation in S. cerevisiae are the N-terminal acetyltransferases...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2023-01-26 | PXD039544 | Pride
Natc N-terminal acetylation N-alpha-acetyltransferase 30 (naa30) Saccharomyces cerevisiae N-terminal acetylome N-terminal cofradic N-terminomics. 
ProteomicsPositional proteomics reveals differences in N-terminal proteoform stability.
To understand the impact of alternative translation initiation on a proteome, we performed the first large-scale study of protein turnover rates in which we distinguish between N-terminal proteoforms pointing to translation initiation events. Using pulsed SILAC combined with N-terminal COFRADIC we m...
ORGANISM(S): Homo sapiens (Human) 
2013-03-14 | PXD002091 | Pride
Nt-acetylation Protein stability Alternative translation initiation Initiator methionine processing Protein turnover N-terminal proteoform Human N-terminal cofradic 
ProteomicsSystem-wide analyses reveal essential roles of N-terminal protein modification in bacterial physiology
Removal of the N-terminal formyl group on nascent proteins by peptide deformylase (PDF) is the most prevalent protein modification in bacteria that impacts over 90% of the proteome. PDF is essential and a critical target of antibiotic development; however, its role in bacterial physiology remains a ...
ORGANISM(S): Escherichia coli 
2022-07-20 | PXD032725 | Pride
Peptide deformylase N-terminal protein modification Membrane potential Mass spectrometry Ribosome profiling Protein biogenesis 
GenomicsSystem-wide analyses reveal essential roles of N-terminal protein modification in bacterial physiology
System-wide analyses reveal essential roles of N-terminal protein modification in bacterial physiology
PRJNA819450 | ENA
ProteomicsPositional proteomics reveals differences in N-terminal proteoform stability.
To understand the impact of alternative translation initiation on a proteome, we performed the first large-scale study of protein turnover rates in which we distinguish between N-terminal proteoforms pointing to translation initiation events. Using pulsed SILAC combined with N-terminal COFRADIC we m...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2019-03-13 | MSV000083565 | MassIVE
ProteomicsAn OMICS perspective on N-terminal Methionine Excision
Excision of the N-terminal initiator methionine (iMet) from nascent peptide chains is an essential and omnipresent protein modification carried out by Methionine aminopetidases (MetAPs) and accounting for a major source of N-terminal proteoform diversity. While MetAP2 is known to be implicated in pr...
ORGANISM(S): Homo sapiens (Human) 
2018-01-10 | PXD006638 | Pride
Metap Metap1 Shotgun N-terminal proteomics Imet excision 
TranscriptomicsGenome-wide search for novel human uORFs and N-terminal protein extensions using ribosomal footprinting
So far, the annotation of translation initiation sites (TISs) has been based mostly upon bioinformatics rather than experimental evidence. We adapted ribosomal footprinting to puromycin-treated cells to generate a transcriptome-wide map of TISs in a human monocytic cell line. A neural network was tr...
ORGANISM(S): Homo sapiens 
2012-08-08 | E-GEOD-39561 | biostudies-arrayexpress
ProteomicsChemical proteomics profiling of N-terminal and lysine acetyltransferases
Acetylation of amino groups is a prevalent protein modification in all kingdoms of life. Acetyl groups are transferred from Coenzyme A (CoA) to protein N-termini and lysine side chains by N-terminal acetyltransferases (NATs) and lysine acetyltransferases (KATs), respectively. Building on lysine-CoA ...
ORGANISM(S): Homo Sapiens (human) 
2021-04-14 | PXD018544 | JPOST Repository
ProteomicsDiscovering the N-terminal Methylome by the Repurposing of Proteomic Datasets
Protein ⍺-N-methylation is a cryptic and relatively unexplored post-translational modification involving the covalent addition of methyl groups to the free a-amino group at protein N-termini. To systematically explore the extent of ⍺-N-terminal methylation in yeast and humans, we utilized a repurpos...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2021-05-26 | PXD022833 | Pride
Proteomics Post-translational modification Repurposing ⍺-n-terminal methylation 
ProteomicsMetabolic regulation of N-terminal acetylation in yeast
N-terminal (Nt) acetylation, catalyzed by N-terminal acetyltransferases (NATs), has emerged as an important co-translational modification in eukaryotes, and involves the transfer of the acetyl moiety from acetyl-CoA (Ac-CoA) to the α-amino group of a nascent polypeptide. Here, we report the first gl...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2018-09-07 | PXD004326 | Pride
Metabolism Acetyl coenzyme a Saccharomyces cerevisiae N-terminal acetylation N-terminomics 
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