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    Please use this identifier to cite or link to this item: http://asiair.asia.edu.tw/ir/handle/310904400/4575


    Title: Crystal structure of the human FOXO3a-DBD/DNA complex suggests the effects of post-translational modification
    Authors: Tsai, K. L.;Sun, Y-J;Huang, C-Y;Yang J-Y;Mien-Chie Hung;Hsiao, C-D
    Date: 2007-10
    Issue Date: 2009-11-27 13:56:53 (UTC+8)
    Publisher: Asia University
    Abstract: FOXO3a is a transcription factor of the FOXO family. The FOXO proteins participate in multiple signaling pathways, and their transcriptional activity is regulated by several post-translational mechanisms, including phosphorylation, acetylation and ubiquitination. Because these post-translational modification sites are located within the C-terminal basic region of the FOXO DNA-binding domain (FOXO-DBD), it is possible that these post-translational modifications could alter the DNA-binding characteristics. To understand how FOXO mediate transcriptional activity, we report here the 2.7 ? crystal structure of the DNA-binding domain of FOXO3a (FOXO3a-DBD) bound to a 13-bp DNA duplex containing a FOXO consensus binding sequence (GTAAACA). Based on a unique structural feature in the C-terminal region and results from biochemical and mutational studies, our studies may explain how FOXO-DBD C-terminal phosphorylation by protein kinase B (PKB) or acetylation by cAMP-response element binding protein (CBP) can attenuate the DNA-binding activity and thereby reduce transcriptional activity of FOXO proteins. In addition, we demonstrate that the methyl groups of specific thymine bases within the consensus sequence are important for FOXO3a-DBD recognition of the consensus binding site.
    Relation: NUCLEIC ACIDS RESEARCH 35(20):6984-6994
    Appears in Collections:[生物科技學系] 期刊論文

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