The dual methyltransferase METTL13 targets N terminus and Lys55 of eEF1A and modulates codon-specific translation rates

@article{Jakobsson2018TheDM,
  title={The dual methyltransferase METTL13 targets N terminus and Lys55 of eEF1A and modulates codon-specific translation rates},
  author={Magnus E. Jakobsson and Jędrzej M. Małecki and Levon Halabelian and Benedikt S Nilges and Rita Pinto and Srikanth Kudithipudi and Stephanie Munk and Erna Davydova and Fawzi Rahmadiyan Zuhairi and Cheryl H. Arrowsmith and Albert Jeltsch and Sebastian A. Leidel and Jesper Velgaard Olsen and P{\aa}l {\O}. Falnes},
  journal={Nature Communications},
  year={2018},
  volume={9}
}
Eukaryotic elongation factor 1 alpha (eEF1A) delivers aminoacyl-tRNA to the ribosome and thereby plays a key role in protein synthesis. Human eEF1A is subject to extensive post-translational methylation, but several of the responsible enzymes remain unknown. Using a wide range of experimental approaches, we here show that human methyltransferase (MTase)-like protein 13 (METTL13) contains two distinct MTase domains targeting the N terminus and Lys55 of eEF1A, respectively. Our biochemical and… 
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  • Biology
    FASEB journal : official publication of the Federation of American Societies for Experimental Biology
  • 2019
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TLDR
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