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...
Topics
- Acetyltransferases
- Amino Acid Sequence
- Amino Acids
- Catalysis
- Cross-Linking Reagents
- Cytosol
- Fungal Proteins
- HSP70 Heat-Shock Proteins
- Models, Biological
- Molecular Sequence Data
- N-Terminal Acetyltransferase A
- Peptides
- Phenotype