Molecular characterization of the zinc finger transcription factor, Osterix.

Molecular characterization of the zinc finger transcription factor, Osterix.
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DOI:
10.3892/ijmm.17.3.425
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发表时间:
2006-03
影响因子:
5.4
通讯作者:
M. Hatta;Y. Yoshimura;Y. Deyama;A. Fukamizu;Kuniaki Suzuki
M. Hatta;Y. Yoshimura;Y. Deyama;A. Fukamizu;Kuniaki Suzuki
中科院分区:
医学3区
文献类型:
--
作者:
M. Hatta;Y. Yoshimura;Y. Deyama;A. Fukamizu;Kuniaki Suzuki

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Osterix被鉴定为在成骨细胞中表达骨形成所需的转录因子。然而,Osterix的基因调控的分子机制仍然难以捉摸。在这项研究中,我们研究了Osterix的反式激活特性,通过使用Gal 4融合系统报告分析。我们确定了Osterix的反式激活结构域,它含有高脯氨酸和甘氨酸残基,在哺乳动物和酵母细胞中具有激活特性。GST-下拉分析显示,基础转录因子,TF-IIB,但不是TBP,结合到反式激活结构域。此外,我们发现Osterix与染色质重塑因子,Brg-1,通过其C-末端锌指结构域在体内和体外相互作用。这些发现表明,Osterix具有与转录介导因子相关的功能结构域,并在细胞核中起转录激活剂的作用。
Osterix was identified as a transcription factor expressing, in osteoblasts, required for bone formation. However, the molecular mechanisms of the gene regulation by Osterix remain elusive. In this study, we examined the transactivation property of Osterix by using the Gal4 fusion system reporter assay. We identified the transactivation domain of Osterix, which contains high proline and glycine residues and has an activation property in mammalian and yeast cells. The GST-pull down analysis revealed that the basal transcription factor, TF-IIB, but not TBP, binds to the transactivation domain. Furthermore, we found that Osterix interacts with chromatin remodeling factor, Brg-1, through its C-terminal zinc finger domain in vivo and in vitro. These findings suggest that Osterix possesses functional domains which associate with transcription mediated factors and functions as a transcriptional activator in the nucleus.