2. Academic Validation
  3. Protein lysine methyltransferase G9a acts on non-histone targets

Protein lysine methyltransferase G9a acts on non-histone targets

  • Nat Chem Biol. 2008 Jun;4(6):344-6. doi: 10.1038/nchembio.88.
Philipp Rathert 1,  Arunkumar Dhayalan,  Marie Murakami,  Xing Zhang,  Raluca Tamas,  Renata Jurkowska,  Yasuhiko Komatsu,  Yoichi Shinkai,  Xiaodong Cheng,  Albert Jeltsch
Affiliations

Affiliation

  • 1 Biochemistry Laboratory, School of Engineering and Science, Jacobs University Bremen, Campus Ring 1, 28759 Bremen, Germany.
PMID: 18438403 DOI: 10.1038/nchembio.88
Abstract

By methylation of peptide arrays, we determined the specificity profile of the protein methyltransferase G9a. We show that it mostly recognizes an Arg-Lys sequence and that its activity is inhibited by methylation of the arginine residue. Using the specificity profile, we identified new non-histone protein targets of G9a, including CDYL1, WIZ, ACINUS and G9a (automethylation), as well as Peptides derived from CSB. We demonstrate potential downstream signaling pathways for methylation of non-histone proteins.

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