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.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 12 print issues and online access
$259.00 per year
only $21.58 per issue
Rent or buy this article
Prices vary by article type
from$1.95
to$39.95
Prices may be subject to local taxes which are calculated during checkout
References
Chuikov, S. et al. Nature 432, 353–360 (2004).
Huang, J. et al. Nature 444, 629–632 (2006).
Shi, X. et al. Mol. Cell 27, 636–646 (2007).
Rathert, P. et al. Nat. Chem. Biol. 4, 344–346 (2008).
Chin, H.G. et al. Nucleic Acids Res. 35, 7313–7323 (2007).
Sampath, S.C. et al. Mol. Cell 27, 596–608 (2007).
Frank, R. Tetrahedron 48, 9217–9232 (1992).
Hilpert, K., Winkler, D.F. & Hancock, R.E. Nat. Protoc. 2, 1333–1349 (2007).
Chin, H.G. et al. Biochemistry 44, 12998–13006 (2005).
Shi, Y. et al. Nature 422, 735–738 (2003).
Tachibana, M. et al. Genes Dev. 19, 815–826 (2005).
Collins, R.E. et al. Nat. Struct. Mol. Biol. 15, 245–250 (2008).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Trojer, P., Reinberg, D. A gateway to study protein lysine methylation. Nat Chem Biol 4, 332–334 (2008). https://doi.org/10.1038/nchembio0608-332
Issue Date:
DOI: https://doi.org/10.1038/nchembio0608-332