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

Top

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.

Top
  1. Biochemistry Laboratory, School of Engineering and Science, Jacobs University Bremen, Campus Ring 1, 28759 Bremen, Germany.
  2. 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.
  3. Department of Biochemistry, Emory University School of Medicine, 1510 Clifton Road, Atlanta, Georgia 30322, USA.
  4. Biochemistry and Cell Biology Program, School of Engineering and Science, Jacobs University Bremen, Campus Ring 1, 28759 Bremen, Germany.
  5. 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



MORE ARTICLES LIKE THIS

These links to content published by NPG are automatically generated.

NEWS AND VIEWS

A gateway to study protein lysine methylation

Nature Chemical Biology News and Views (01 Jun 2008)

Tudor hooks up with DNA repair

Nature Structural & Molecular Biology News and Views (01 Feb 2007)

See all 3 matches for News And Views

Extra navigation

Subscribe to Nature Chemical Biology

Subscribe

Open Innovation Challenges

naturejobs