Identification and Characterization of a Novel Evolutionarily Conserved Lysine-specific Methyltransferase Targeting Eukaryotic Translation Elongation Factor 2 (eEF2)*

@article{Davydova2014IdentificationAC,
  title={Identification and Characterization of a Novel Evolutionarily Conserved Lysine-specific Methyltransferase Targeting Eukaryotic Translation Elongation Factor 2 (eEF2)*},
  author={Erna Davydova and Angela Yeuan Yen Ho and Jędrzej M. Małecki and Anders Moen and Jorrit M. Enserink and Magnus E. Jakobsson and Christoph Loenarz and P{\aa}l {\O}. Falnes},
  journal={The Journal of Biological Chemistry},
  year={2014},
  volume={289},
  pages={30499 - 30510}
}
Background: The function of many proteins is regulated through post-translational methylation. Results: The previously uncharacterized human methyltransferase FAM86A and its yeast homologue Yjr129c methylate eukaryotic translation elongation factor 2 (eEF2), altering translational frameshifting. Conclusion: Evolutionarily conserved FAM86A methyltransferase modulates the function of eEF2. Significance: The activity of a novel protein-modifying enzyme is discovered and is shown to have functional… 
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TLDR
It is demonstrated that an uncharacterized human 7BS MTase currently annotated as part of the endothelin converting enzyme 2, but which should be considered a separate enzyme efficiently methylates K36 in eukaryotic translation elongation factor 1 alpha (eEF1A) in vitro and in vivo.
The dual methyltransferase METTL13 targets N terminus and Lys55 of eEF1A and modulates codon-specific translation rates
TLDR
The authors identify METTL13 as an eEF1A methyltransferase with dual specificity, which is involved in the codon-specific modulation of mRNA translation.
Novel N-terminal and Lysine Methyltransferases That Target Translation Elongation Factor 1A in Yeast and Human*
TLDR
A new eukaryotic protein N-terminal methyltransferase is reported, Saccharomyces cerevisiae YLR285W, which methylates eEF1A at a previously undescribed high-stoichiometry N-Terminal site and the adjacent lysine and is named Efm7.
A new type of protein lysine methyltransferase trimethylates Lys-79 of elongation factor 1A.
The novel lysine specific methyltransferase METTL21B affects mRNA translation through inducible and dynamic methylation of Lys-165 in human eukaryotic elongation factor 1 alpha (eEF1A)
TLDR
It is demonstrated, using a wide range of in vitro and in vivo approaches, that the previously uncharacterized human methyltransferase METTL21B specifically targets Lys-165 in eEF1A in an aminoacyl-tRNA- and GTP-dependent manner and shows that this modification is dynamic, inducible and likely of regulatory importance.
Evolutionary insights into Trm112-methyltransferase holoenzymes involved in translation between archaea and eukaryotes
TLDR
It is unraveled that methyltransferases are also privileged Trm112 partners in archaea and that this Trm 112 network is much more complex than anticipated from eukaryotic studies.
Human METTL18 is a histidine-specific methyltransferase that targets RPL3 and affects ribosome biogenesis and function
TLDR
METTL18 is established as the second human histidine-specific protein MTase, and its functional relevance is demonstrated, indicating that METTL18-mediated methylation of RPL3 is important for optimal ribosome biogenesis and function.
Human METTL20 Is a Mitochondrial Lysine Methyltransferase That Targets the β Subunit of Electron Transfer Flavoprotein (ETFβ) and Modulates Its Activity*
TLDR
The present study establishes METTL20 as the first human KMT localized to mitochondria and suggests that it may regulate cellular metabolism through modulating the interaction between its substrate ETFβ and dehydrogenases.
Found in Translation: The Search for Functional Roles of Translation Elongation Factor Methylation and the Discovery of a Novel Type of Protein Methylation
TLDR
This dissertation describes the attempts made to identify this new substrate and modification for protein methylation in Saccharomyces cerevisiae but as of yet, it remains elusive.
Characterization of Protein Methyltransferases Rkm1, Rkm4, Efm4, Efm7, Set5 and Hmt1 Reveals Extensive Post-Translational Modification.
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