Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 288, Issue 23, Pages 16430-16437Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M112.446849
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Funding
- Chinese Ministry of Science and Technology [2009CB825502, 2012CB917202]
- National Natural Science Foundation of China [31171241, 30970576]
- Ph.D. Program Foundation of the Ministry of Education of China [20113402110033]
- 100 Talents Program of the Chinese Academy of Sciences
- NIAMS, National Institutes of Health [AR061590]
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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 winged helix-turn-helix 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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