Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Expanded in vivo substrate profile of the yeast N-terminal acetyltransferase NatC.

The Journal of biological chemistry - 1 Feb 2023

Van Damme Petra, Osberg Camilla, Jonckheere Veronique, Glomnes Nina, Gevaert Kris, Arnesen Thomas, Aksnes Henriette

Abstract excerpt

N-terminal acetylation is a conserved protein modification among eukaryotes. The yeast Saccharomyces cerevisiae is a valuable model system for studying this modification. The bulk of protein N-terminal acetylation in S. cerevisiae is catalyzed by the N-terminal acetyltransferases NatA, NatB, and NatC. Thus far, proteome-wide identification of the in vivo protein substrates of yeast NatA and NatB has been...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Acetylation
Share to Chromatography, Liquid

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Conserved Sequence

Share to Genetic Complementation Test

Share to Methionine

Share to Protein Processing, Post-Translational

Share to Saccharomyces cerevisiae

Share to Substrate Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 36567016
DOI: 10.1016/j.jbc.2022.102824
PMCID: PMC9867985

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Expanded in vivo substrate profile of the yeast N-terminal acetyltransferase NatC.PMID 36567016Read ↗

A Saccharomyces cerevisiae model reveals in vivo functional impairment of the Ogden syndrome N-terminal acetyltransferase NAA10 Ser37Pro mutant.Semantic proximity Read ↗

Proteomics analyses reveal the evolutionary conservation and divergence of N-terminal acetyltransferases from yeast and humansSemantic proximity Read ↗

Human NAA30 can rescue yeast mak3∆ mutant growth phenotypes.Semantic proximity Read ↗

NATs at a glanceSemantic proximity Read ↗

Perturbation of the yeast N-acetyltransferase NatB induces elevation of protein phosphorylation levels.Semantic proximity Read ↗

N-Terminal Acetyltransferase Naa40p Whereabouts Put into N-Terminal Proteoform PerspectiveSemantic proximity Read ↗

NatF Contributes to an Evolutionary Shift in Protein N-Terminal Acetylation and Is Important for Normal Chromosome SegregationSemantic proximity Read ↗

Functional mapping of N-terminal residues in the yeast proteome uncovers novel determinants for mitochondrial protein importSemantic proximity Read ↗

NatC Nalpha-terminal acetyltransferase of yeast contains three subunits, Mak3p, Mak10p, and Mak31p.Semantic proximity Read ↗

Big fish, little fish: N-terminal acetyltransferase Naa40p proteoforms caught in the actSemantic proximity Read ↗

The biological functions of Naa10 – from amino-terminal acetylation to human diseaseSemantic proximity Read ↗

NAA10 p.(D10G) and NAA10 p.(L11R) Variants Hamper Formation of the NatA N-Terminal Acetyltransferase Complex.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.