• Reference Type: Published Erratum
  Porras-Yakushi TR, et al. (2008) Correction: A novel SET domain methyltransferase in yeast: Rkm2-dependent trimethylation of ribosomal protein L12ab at the N terminus. J Biol Chem 283 (22):15512
  • SGD Paper

  In this study, we identified the Saccharomyces cerevisiae RKM2 gene encoding a methyltransferase that catalyzes the trimethylation of a lysine residue in the N terminus of the large subunit ribosomal protein Rpl12ab. Based on the previous identification of dimethyllysine and trimethyllysine in this protein (Lhoest, J., Lobet, Y., Costers, E., and Colson, C. (1984) Eur. J. Biochem. 141, 585-590) as well as our mass spectrometry and amino acid analyses, we suggested that Rpl12ab was modified by dimethylation at Lys-3 catalyzed by an as yet unidentified enzyme and by trimethylation at Lys-10 by Rkm2. Recently, two published articles have suggested that the Arabidopsis thaliana (Carroll, A. J., Heazlewood, J. L., Ito, J., and Millar, A. H. (2008) Mol. Cell. Proteomics 7, 347-369) and Schizosaccharomyces pombe (Sadaie, M., Shinmyozu, K., and Nakayama, J. (2008) J. Biol. Chem. 283, 7185-7195) homologs of S. cerevisiae Rpl12ab are modified by the dimethylation of the N-terminal proline residue and by the trimethylation of Lys-3. The authors of the Arabidopsis study pointed out that the mass spectral data presented in our work are consistent with the S. cerevisiae protein having the same pattern of methylation as the A. thaliana protein. We have now re-evaluated our mass spectral data and agree that our data are consistent with the dimethylation of Pro-1 and the Rkm2-dependent trimethylation of Lys-3, although the evidence presented in our study does support at least a minor degree of alternative trimethylation at Lys-10 (b8, b9, and y9 ions in the wild-type mass spectrum in Fig. 4). Additional experiments performed in our laboratories by Kristofor Webb (to be published) have confirmed that the major trimethylation site is at Lys-3 rather than at Lys-10. These results suggest that the Rpl12ab proteins in S. cerevisiae, S. pombe, and A. thaliana all share the same modifications at the N terminus: a dimethylproline residue at position 1 and a trimethyllysine residue at position 3. A corrected title is shown above.

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