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Nature Chemical Biology 4, 332 - 334 (2008)
doi:10.1038/nchembio0608-332
A gateway to study protein lysine methylation
Patrick Trojer1 & Danny Reinberg1
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Patrick Trojer is in the Department of Biochemistry and Danny Reinberg is in the Department of Biochemistry and the Howard Hughes Medical Institute, New York University, School of Medicine, 522 First Avenue, Smilow Research Building, New York, New York 10016, USA.
e-mail: reinbd01@med.nyu.edu
Abstract
Lysine methyltransferases are well-known regulators of transcription through their methylation of histone lysine residues. Now high-throughput peptide arrays reveal non-histone substrates of G9a/KMT3C, which was previously known as a euchromatic histone H3K9-specific methyltransferase.
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