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Protein lysine methyltransferase G9a acts on non-histone targets.

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.

SUBMITTER: Rathert P

PROVIDER: S-EPMC2696268 | biostudies-literature | 2008 Jun

REPOSITORIES: biostudies-literature

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Protein lysine methyltransferase G9a acts on non-histone targets.

Rathert Philipp P Dhayalan Arunkumar A Murakami Marie M Zhang Xing X Tamas Raluca R Jurkowska Renata R Komatsu Yasuhiko Y Shinkai Yoichi Y Cheng Xiaodong X Jeltsch Albert A

Nature chemical biology 20080427 6

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-hist ...[more]

PMID: 18438403

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