title: N(α)-Acetylation of yeast ribosomal proteins and its effect on protein synthesis.
abstract: N(α)-Acetyltransferases (NATs) cause the N(α)-acetylation of the majority of eukaryotic proteins during their translation, although the functions of this modification have been largely unexplored. In yeast (Saccharomyces cerevisiae), four NATs have been identified: NatA, NatB, NatC, and NatD. In this study, the N(α)-acetylation status of ribosomal protein was analyzed using NAT mutants combined with two-dimensional difference gel electrophoresis (2D-DIGE) and mass spectrometry (MS). A total of 60 ribosomal proteins were identified, of which 17 were N(α)-acetylated by NatA, and two by NatB. The N(α)-acetylation of two of these, S17 and L23, by NatA was not previously observed. Furthermore, we tested the effect of ribosomal protein N(α)-acetylation on protein synthesis using the purified ribosomes from each NAT mutant. It was found that the protein synthesis activities of ribosomes from NatA and NatB mutants were decreased by 27% and 23%, respectively, as compared to that of the normal strain. Furthermore, we have shown that ribosomal protein N(α)-acetylation by NatA influences translational fidelity in the presence of paromomycin. These results suggest that ribosomal protein N(α)-acetylation is necessary to maintain the ribosome's protein synthesis function.
authors.affiliation: Graduate School of Nanobioscience, Yokohama City University, Tsurumi, Yokohama, Japan.
authors.forename: Masahiro
authors.initials: M
authors.lastname: Kamita
authors.forename: Yayoi
authors.initials: Y
authors.lastname: Kimura
authors.forename: Yoko
authors.initials: Y
authors.lastname: Ino
authors.forename: Roza M
authors.initials: RM
authors.lastname: Kamp
authors.forename: Bogdan
authors.initials: B
authors.lastname: Polevoda
authors.forename: Fred
authors.initials: F
authors.lastname: Sherman
authors.forename: Hisashi
authors.initials: H
authors.lastname: Hirano
mesh_terms: D000107:Acetylation; D000123:Acetyltransferases / Q000032:analysis / Q000235:genetics / Q000378:metabolism* / Q000502:physiology; D000595:Amino Acid Sequence; D001483:Base Sequence; D049109:Cell Proliferation; D005656:Fungal Proteins / Q000032:analysis / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D030781:Organisms, Genetically Modified; D011132:Polyribosomes / Q000235:genetics / Q000378:metabolism; D014176:Protein Biosynthesis / Q000235:genetics / Q000502:physiology; D011499:Protein Processing, Post-Translational / Q000235:genetics / Q000502:physiology*; D012269:Ribosomal Proteins / Q000032:analysis / Q000235:genetics / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000254:growth & development / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism; D057825:Two-Dimensional Difference Gel Electrophoresis
chemical_list: D005656:Fungal Proteins; D012269:Ribosomal Proteins; D029701:Saccharomyces cerevisiae Proteins; D000123:Acetyltransferases