Identification of trimethylated histone H3 lysine 27 binding proteins

• Main Author: Berger, Hanna Heidi
• Other Authors: Su I-Hsin
• Format: Theses and Dissertations
• Language: English
• Published: 2016
• Subjects: DRNTU::Science::Biological sciences
• Online Access: http://hdl.handle.net/10356/68858
• Institution: Nanyang Technological University

Identification of Trimethylated Histone H3 Lysine 27 Binding Proteins We report a novel lysine methyl-binding protein, which selectively recognizes the EZH2-mediated H3K27me3 signal through its C-terminal PHD domain. This novel protein is primarily located in the cytosol and is co-localized with actin-rich regions. Overexpression of this novel protein leads to increased cell spreading, increased formation of adhesion structures and decreased cell motility. This phenotypic observation is supported by iTRAQ proteomic analysis, RT-qPCR and immunoblotting, which identified multiple cytoskeletal and cell adhesion related proteins to be upregulated. Furthermore, this novel protein partially counteracts the effect of EZH2 on cell spreading. Here, it may either bind to methylated cytosolic proteins or regulate the expression of genes by interacting with H3K27me3. We are currently focusing on the identification of trimethylated proteins that interact with this novel protein.