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Molecular and Cellular Biology, October 2003, p. 7403-7414, Vol. 23, No. 20
0270-7306/03/$08.00+0     DOI: 10.1128/MCB.23.20.7403-7414.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

The Yeast N{alpha}-Acetyltransferase NatA Is Quantitatively Anchored to the Ribosome and Interacts with Nascent Polypeptides

Matthias Gautschi,1,{dagger} Sören Just,1 Andrej Mun,1 Suzanne Ross,1 Peter Rücknagel,1 Yves Dubaquié,2 Ann Ehrenhofer-Murray,3 and Sabine Rospert1,4*

Max Planck Research Unit "Enzymology of Protein Folding," D-06120 Halle,1 Institut für Biochemie und Molekularbiologie, Universität Freiburg, D-79104 Freiburg,4 Otto Warburg Laboratory, Max Planck Institute of Molecular Genetics, D-14195 Berlin, Germany,3 Proteomics Department, Bristol-Myers Squibb, Princeton, New Jersey 08543-54002

Received 16 April 2003/ Returned for modification 29 May 2003/ Accepted 8 July 2003

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 and is thought to act cotranslationally. We found that NatA was quantitatively bound to ribosomes via Nat1p and contained a previously unrecognized third subunit, the N{alpha}-acetyltransferase homologue Nat5p. Nat1p not only anchored Ard1p and Nat5p to the ribosome but also was in close proximity to nascent polypeptides, independent of whether they were substrates for N{alpha}-acetylation or not. Besides Nat1p, NAC (nascent polypeptide-associated complex) and the Hsp70 homologue Ssb1/2p interact with a variety of nascent polypeptides on the yeast ribosome. A direct comparison revealed that Nat1p required longer nascent polypeptides for interaction than NAC and Ssb1/2p. {Delta}nat1 or {Delta}ard1 deletion strains were temperature sensitive and showed derepression of silent mating type loci while {Delta}nat5 did not display any obvious phenotype. Temperature sensitivity and derepression of silent mating type loci caused by {Delta}nat1 or {Delta}ard1 were partially suppressed by overexpression of SSB1. The combination of data suggests that Nat1p presents the N termini of nascent polypeptides for acetylation and might serve additional roles during protein synthesis.

* Corresponding author. Mailing address: Institut für Biochemie undMolekularbiologie, Universität Freiburg, Hermann-Herder-Strasse 7, D-79104 Freiburg, Germany. Phone: 49-761-203-5224. Fax: 49-761-203-5261. E-mail: Sabine.Rospert{at}biochemie.uni-freiburg.de.

{dagger} Present address: Swiss Federal Institute of Technology Zürich, ETH Hönggerberg, CH-8093 Zürich, Switzerland.

Molecular and Cellular Biology, October 2003, p. 7403-7414, Vol. 23, No. 20
0022-538X/03/$08.00+0     DOI: 10.1128/MCB.23.20.7403-7414.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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