Brief Communication abstract
Nature Chemical Biology 4, 344 - 346 (2008)
Published online: 27 April 2008 | doi:10.1038/nchembio.88
Protein lysine methyltransferase G9a acts on non-histone targets
Philipp Rathert1, Arunkumar Dhayalan1, Marie Murakami2, Xing Zhang3, Raluca Tamas1,4, Renata Jurkowska1, Yasuhiko Komatsu5, Yoichi Shinkai2, Xiaodong Cheng3 & Albert Jeltsch1
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.
- Biochemistry Laboratory, School of Engineering and Science, Jacobs University Bremen, Campus Ring 1, 28759 Bremen, Germany.
- Research Center for Infectious Diseases, Institute for Virus Research and Graduate School of Biostudies, Kyoto University, 53 Shogoin, Kawara-cho, Sakyo-ku, Kyoto, Kyoto 606-8507, Japan.
- Department of Biochemistry, Emory University School of Medicine, 1510 Clifton Road, Atlanta, Georgia 30322, USA.
- Biochemistry and Cell Biology Program, School of Engineering and Science, Jacobs University Bremen, Campus Ring 1, 28759 Bremen, Germany.
- R&D Division, Advanced Life Science Institute Inc., 2-10-23, Maruyamadai, Wako, Saitama 351-0112, Japan.
Correspondence to: Albert Jeltsch1 e-mail: a.jeltsch@jacobs-university.de
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