Ubiquitination of Lysine 867 of the Human SETDB1 Protein Upregulates Its Histone H3 Lysine 9 (H3K9) Methyltransferase Activity

• DOI: 10.1371/journal.pone.0165766
• Publication Date: 2016-10-31T13:38:25Z
• Authors: Kenji Ishimoto; Natsuko Kawamata; Yoshie Uchihara; Moeka Okubo; Reiko Fujimoto; Eiko Gotoh; Keisuke Kakinouchi; Eiichi Mizohata; Nobumasa Hino; Yoshiaki Okada; Yasuhiro Mochizuki; Toshiya Tanaka; Takao Hamakubo; Juro Sakai; Tatsuhiko Kodama; Tsuyoshi Inoue; Keisuke Tachibana; Takefumi Doi
• Keywords: Histone Methylation

Posttranslational modifications (PTMs) of proteins play a crucial role in regulating protein-protein interactions, enzyme activity, subcellular localization, and stability the protein. SET domain, bifurcated 1 (SETDB1) is histone methyltransferase that regulates methylation H3 on lysine 9 (H3K9), gene silencing, transcriptional repression. The C-terminal region SETDB1 key site for PTMs, essential its activity mammalian insect cells. In this study, we aimed to evaluate more precisely effect PTMs H3K9 SETDB1. Using mass spectrometry analysis, show human purified from cells ubiquitinated. We also demonstrate ubiquitination 867 necessary full Finally, expression target gene, serpin peptidase inhibitor, clade E, member (SERPINE1) by methylating H3K9. These results suggest at controls activating activity.