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Eukaryotic Cell, February 2006, p. 368-378, Vol. 5, No. 2
1535-9778/06/$08.00+0     doi:10.1128/EC.5.2.368-378.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Physiological Importance and Identification of Novel Targets for the N-Terminal Acetyltransferase NatB{dagger}

Robert Caesar,* Jonas Warringer, and Anders Blomberg* Received 15 September 2005/ Accepted 16 December 2005

The N-terminal acetyltransferase NatB in Saccharomyces cerevisiae consists of the catalytic subunit Nat3p and the associated subunit Mdm20p. We here extend our present knowledge about the physiological role of NatB by a combined proteomics and phenomics approach. We found that strains deleted for either NAT3 or MDM20 displayed different growth rates and morphologies in specific stress conditions, demonstrating that the two NatB subunits have partly individual functions. Earlier reported phenotypes of the nat3{Delta} strain have been associated with altered functionality of actin cables. However, we found that point mutants of tropomyosin that suppress the actin cable defect observed in nat3{Delta} only partially restores wild-type growth and morphology, indicating the existence of functionally important acetylations unrelated to actin cable function. Predicted NatB substrates were dramatically overrepresented in a distinct set of biological processes, mainly related to DNA processing and cell cycle progression. Three of these proteins, Cac2p, Pac10p, and Swc7p, were identified as true NatB substrates. To identify N-terminal acetylations potentially important for protein function, we performed a large-scale comparative phenotypic analysis including nat3{Delta} and strains deleted for the putative NatB substrates involved in cell cycle regulation and DNA processing. By this procedure we predicted functional importance of the N-terminal acetylation for 31 proteins.

* Corresponding author. Mailing address for Robert Caesar: Department of Cell and Molecular Biology, Lundberg Laboratory, Göteborg University, Medicinaregatan 9c, 413 90 Göteborg, Sweden. Phone: 46-31-7732568. Fax: 46-31-7732599. E-mail: robert.svensson{at}gmm.gu.se. Mailing address for Anders Blomberg: Department of Cell and Molecular Biology, Lundberg Laboratory, Göteborg University, Medicinaregatan 9c, 413 90 Göteborg, Sweden. Phone: 46-31-7732589. Fax: 46-31-7732599. E-mail: anders.blomberg{at}gmm.gu.se.

{dagger} Supplemental material for this article may be found at http://ec.asm.org/.

Eukaryotic Cell, February 2006, p. 368-378, Vol. 5, No. 2
1535-9778/06/$08.00+0     doi:10.1128/EC.5.2.368-378.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.





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Copyright © 2006 by the American Society for Microbiology.