히스톤 메틸전이효소 KODO12의 전사조절작용에 관한 연구

Abstract

Covalent modifications of histones by acetylation, methylation, phosphorylation, and ubiquitilation play important roles in dynamic regulation of gene expression. A large number of histone methyltransferase contain SET(Su(var)3-9, E(z), and trithorax) domain and catalyze Mono-, Di- or Tri-methylation of core histone lysine residues. In this study, we conducted investigation into identification of novel histone methyltransferase KODO12. KODO12 contains bifurcated SET domain and rubis-subs-bind domain. We performed HMTase assay to verify methyltransferase activity of KODO12. Synthesized peptides were used for HMTase assay for identify specificity of KODO12 activity. To confirm effect of histone modification of KODO12 we conducted transient reporter assay. GST -pull down assay and immunoprecipitation assay exhibited interaction between KODO12 and HDAC1. These data elucidates the regulatory role in transcription and cellular effect of KODO12.