A Novel 3-Methylhistidine Modification of Yeast Ribosomal Protein Rpl3 Is Dependent upon the YIL110W Methyltransferase*

@article{Webb2010AN3,
  title={A Novel 3-Methylhistidine Modification of Yeast Ribosomal Protein Rpl3 Is Dependent upon the YIL110W Methyltransferase*},
  author={Kristofor J. Webb and Cecilia I. Zurita-Lopez and Qais Al-Hadid and Arthur Laganowsky and Brian D. Young and Rebecca S. Lipson and Puneet Souda and Kym Francis Faull and Julian P. Whitelegge and Steven G. Clarke},
  journal={The Journal of Biological Chemistry},
  year={2010},
  volume={285},
  pages={37598 - 37606}
}
We have shown that Rpl3, a protein of the large ribosomal subunit from baker's yeast (Saccharomyces cerevisiae), is stoichiometrically monomethylated at position 243, producing a 3-methylhistidine residue. This conclusion is supported by top-down and bottom-up mass spectrometry of Rpl3, as well as by biochemical analysis of Rpl3 radiolabeled in vivo with S-adenosyl-l-[methyl-3H]methionine. The results show that a +14-Da modification occurs within the GTKKLPRKTHRGLRKVAC sequence of Rpl3. Using… 

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