ArticleThe Journal of biological chemistry2013
Structural insights into histone demethylase NO66 in interaction with osteoblast-specific transcription factor osterix and gene repression.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 16 citations in OpenAlex.
- Mechanisms Regulating Muscle Protein Synthesis in CKD.Journal of the American Society of Nephrology : JASN · 2020Article
- The emerging roles of ribosomal histidyl hydroxylases in cell biology, physiology and disease.Cellular and molecular life sciences : CMLS · 2018Review
- Developmental Dioxin Exposure Alters the Methylome of Adult Male Zebrafish Gonads.Frontiers in genetics · 2018Article
- Jmjd6, a JmjC Dioxygenase with Many Interaction Partners and Pleiotropic Functions.Frontiers in genetics · 2017Review
- Histone methyltransferases and demethylases: regulators in balancing osteogenic and adipogenic differentiation of mesenchymal stem cells.International journal of oral science · 2015Review
- Structure of the JmjC domain-containing protein NO66 complexed with ribosomal protein Rpl8.Acta crystallographica. Section D, Biological crystallography · 2015Article
- Article
- The roles of Jumonji-type oxygenases in human disease.Epigenomics · 2014Review
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
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 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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Registered trials
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