期刊
JOURNAL OF PROTEOMICS
卷 74, 期 4, 页码 431-441出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jprot.2010.12.007
关键词
N-alpha-Acetylation; Ribosome; Ribosomal protein; 2D-DIGE
资金
- Special Coordination Funds for Promoting Science and Technology Creation of Innovation Centers for Advanced Interdisciplinary Research Areas
- National Institutes of Health [R01 GM12702]
- Grants-in-Aid for Scientific Research [23701086] Funding Source: KAKEN
N-alpha-Acetyltransferases (NATs) cause the N-alpha-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-alpha-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-alpha-acetylated by NatA, and two by NatB. The N-alpha-acetylation of two of these, S17 and L23, by NatA was not previously observed. Furthermore, we tested the effect of ribosomal protein N-alpha-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-alpha-acetylation by NatA influences translational fidelity in the presence of paromomycin. These results suggest that ribosomal protein N-alpha-acetylation is necessary to maintain the ribosome's protein synthesis function. (C) 2010 Elsevier B.V. All rights reserved.
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