Protein lysine methyltransferase G9a acts on non-histone targets

Philipp Rathert; Arunkumar Dhayalan; Marie Murakami; Xing Zhang; Raluca Tamas; Renata Jurkowska; Yasuhiko Komatsu; Yoichi Shinkai; Xiaodong Cheng; Albert Jeltsch

doi:10.1038/nchembio.88

Protein lysine methyltransferase G9a acts on non-histone targets

Philipp Rathert, Arunkumar Dhayalan, Marie Murakami, Xing Zhang, Raluca Tamas, Renata Jurkowska, Yasuhiko Komatsu, Yoichi Shinkai, Xiaodong Cheng, Albert Jeltsch

Research output: Contribution to journal › Article › peer-review

286 Scopus citations

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.

Original language	English (US)
Pages (from-to)	344-346
Number of pages	3
Journal	Nature Chemical Biology
Volume	4
Issue number	6
DOIs	https://doi.org/10.1038/nchembio.88
State	Published - Jun 2008
Externally published	Yes

ASJC Scopus subject areas

Molecular Biology
Cell Biology

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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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AU - Rathert, Philipp

AU - Dhayalan, Arunkumar

AU - Murakami, Marie

AU - Zhang, Xing

AU - Tamas, Raluca

AU - Jurkowska, Renata

AU - Komatsu, Yasuhiko

AU - Shinkai, Yoichi

AU - Cheng, Xiaodong

AU - Jeltsch, Albert

PY - 2008/6

Y1 - 2008/6

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AB - 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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JO - Nature Chemical Biology

JF - Nature Chemical Biology

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Protein lysine methyltransferase G9a acts on non-histone targets

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