The interaction between Fe65 and Tip60 is regulated by S-nitrosylation on 440 cystein residue of Fe65

Eun Jeoung Lee, Sung Hwa Shin, Sunghee Hyun, Jaesun Chun, Sang Sun Kang
2011 Advances in Biological Chemistry  
The S-Nitrosylation of protein thiol groups by NO is a widely recognized protein modification. The treatment of cells with NOBF4 induces the S-nitrosylation of FE65. In this study, we present evidence showing that FE65 modified by NO (Nitric Oxide) via S-nitrosylation induces functional changes in the protein that inhibits the HAT activity of Tip60. The results of mutational analysis of FE65 demonstrated further that the cysteine residue of FE65 (Cys440) is critical to the process of
more » ... ocess of S-nitrosylation. The mutation of the cysteine residue which completely ablated the S-nitrosylation of FE65 also lost its inhibitory effects on Tip60 HAT activity. Thus, our findings show, for the first time, that the novel regulation mechanism of Tip60 activity may operate via FE65 binding, which is enhanced by S-nitrosylation on the FE65 Cys440 residue. This study describes the interaction between FE65 and Tip60, which is enhanced by a posttranslational modification of FE65 (through S-nitrosylation) by NO, promoting the association of the FE65-Tip60 protein complex and inhibiting both the HAT activity of Tip60 and cell death.
doi:10.4236/abc.2011.13013 fatcat:qrkegvlj7rbufmpunh55ppu2zq