A Newly Uncovered Group of Distantly Related Lysine Methyltransferases Preferentially Interact with Molecular Chaperones to Regulate Their Activity

@article{Cloutier2013ANU,
  title={A Newly Uncovered Group of Distantly Related Lysine Methyltransferases Preferentially Interact with Molecular Chaperones to Regulate Their Activity},
  author={Philippe Cloutier and Mathieu Lavall{\'e}e-Adam and Denis Faubert and Mathieu Blanchette and Benoit Coulombe},
  journal={PLoS Genetics},
  year={2013},
  volume={9}
}
Methylation is a post-translational modification that can affect numerous features of proteins, notably cellular localization, turnover, activity, and molecular interactions. Recent genome-wide analyses have considerably extended the list of human genes encoding putative methyltransferases. Studies on protein methyltransferases have revealed that the regulatory function of methylation is not limited to epigenetics, with many non-histone substrates now being discovered. We present here our… 
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136 Citations

Identification and Characterization of a Novel Human Methyltransferase Modulating Hsp70 Protein Function through Lysine Methylation*
TLDR
It is shown that trimethylation of HSPA8 (Hsc70) has functional consequences, as it alters the affinity of the chaperone for both the monomeric and fibrillar forms of the Parkinson disease-associated protein α-synuclein.
Methylation of human eukaryotic elongation factor alpha (eEF1A) by a member of a novel protein lysine methyltransferase family modulates mRNA translation
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.
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.
A System for Enzymatic Lysine Methylation in a Desired Sequence Context
TLDR
A versatile system for introducing lysine methylation into a desired peptide sequence is described, and the approach should be readily expandable for generating combinatorial libraries of methylated sequences.
Identification and Characterization of a Novel Evolutionarily Conserved Lysine-specific Methyltransferase Targeting Eukaryotic Translation Elongation Factor 2 (eEF2)*
TLDR
The present study establishes the function of the previously uncharacterized MTases FAM86A and Yjr129c, demonstrating that these enzymes introduce a functionally important lysine methylation in eEF2.
Elongation factor methyltransferase 3--a novel eukaryotic lysine methyltransferase.
Protein lysine methylation by seven-β-strand methyltransferases.
TLDR
A number of novel 7BS KMTs have now been discovered, and, in particular, several recently characterized human and yeast members of MTase family 16 (MTF16) have been found to methylate lysines in non-histone proteins.
Regulation of eukaryotic elongation factor 1 alpha (eEF1A) by dynamic lysine methylation
TLDR
It is shown that lysine methylation of eEF1A can be dynamic and inducible, and modulates mRNA translation in a codon-specific fashion.
Selenium-Based S-Adenosylmethionine Analog Reveals the Mammalian Seven-Beta-Strand Methyltransferase METTL10 to Be an EF1A1 Lysine Methyltransferase
TLDR
The utility of the synthetic cofactor ProSeAM as a chemical probe for the identification of non-histone substrates of KMTs of lysine methylation is emphasized.
Methylation of the DNA/RNA-binding protein Kin17 by METTL22 affects its association with chromatin.
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