Protein lysine methyltransferase G9a acts on non-histone targets.
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.
Rathert
Philipp
P
Biochemistry Laboratory, School of Engineering and Science, Jacobs University Bremen, Campus Ring 1, 28759 Bremen, Germany.
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
D000076983:Histone Methyltransferases; D011495:Histone-Lysine N-Methyltransferase / Q000737:chemistry* / Q000378:metabolism; D008745:Methylation; D040081:Protein Array Analysis; D011496:Protein Methyltransferases; D015398:Signal Transduction; D013379:Substrate Specificity
D000076983:Histone Methyltransferases; D011496:Protein Methyltransferases; D011495:Histone-Lysine N-Methyltransferase