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Article

The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides.

Molecular and cellular biology - 1 Oct 2003

Gautschi Matthias, Just Sören, Mun Andrej, Ross Suzanne, Rücknagel Peter, Dubaquié Yves, Ehrenhofer-Murray Ann, Rospert Sabine

Abstract excerpt

The majority of cytosolic proteins in eukaryotes contain a covalently linked acetyl moiety at their very N terminus. The mechanism by which the acetyl moiety is efficiently transferred to a large variety of nascent polypeptides is currently only poorly understood. Yeast N(alpha)-acetyltransferase NatA, consisting of the known subunits Nat1p and the catalytically active Ard1p, recognizes a wide range of sequences...

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Identifiers

PMID: 14517307
DOI: 10.1128/MCB.23.20.7403-7414.2003
PMCID: PMC230319

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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.

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