2013.04.24，我院臧建业教授研究组在Journal of Biological Chemistry上发表论文：
Structural insights into histone demethylase NO66 in interaction with osteoblast specific transcription factor Osterix and gene repression.
作者：陶悦、 吴旻昊 、周星、 殷梧、 胡兵、 de Crombrugghe B, Sinha KM、 臧建业
Abstract
Osterix (Osx) is an osteoblast-specific transcriptional factor and is required for osteoblast differentiation and bone formation. A JmjC domain-containing protein NO66 was previously found to participate in regulation of Osx transcriptional activity and plays an important role in osteoblast differentiation through interaction with Osx. Here we report the crystal structure of NO66 forming in a functional tetramer. A hinge domain links the N-terminal JmjC domain and C-terminal wHTH domain of NO66, and both domains are essential for tetrameric assembly. The oligomerization interface of NO66 interacts with a conserved fragment of Osx. We show that the hinge domain-dependent oligomerization of NO66 is essential for inhibition of Osx-dependent gene activation. Our findings suggest that homo-oligomerization of JmjC domain containing proteins might play a physiological role through interactions with other regulatory factors during gene expression.

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