RESEARCH ARTICLE

Structural studies on MRG701 chromodomain reveal a novel dimerization interface of MRG proteins in green plants

  • Yanchao Liu 1,2 ,
  • Hong Wu 1 ,
  • Yu Yu 3 ,
  • Ying Huang , 1
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  • 1. State Key Laboratory of Molecular Biology, National Center for Protein Science Shanghai, Shanghai Science Research Center, Shanghai Key Laboratory of Molecular Andrology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China
  • 2. University of Chinese Academy of Sciences, Beijing 100049, China
  • 3. State Key Laboratory of Genetic Engineering, Collaborative Innovation Center of Genetics and Development Institute of Plant Biology, School of Life Science, Fudan University, Shanghai 200433, China

Received date: 19 Jun 2016

Accepted date: 26 Jul 2016

Published date: 28 Nov 2016

Copyright

2016 The Author(s) 2016. This article is published with open access at Springerlink.com and journal.hep.com.cn

Abstract

MRG proteins are conserved during evolution in fungi, flies, mammals and plants, and they can exhibit diversified functions. The animal MRGs were found to form various complexes to activate gene expression. Plant MRG1/2 and MRG702 were reported to be involved in the regulation of flowering time via binding to H3K36me3-marked flowering genes. Herein, we determined the crystal structure of MRG701 chromodomain (MRG701CD). MRG701CD forms a novel dimerization fold both in crystal and in solution. Moreover, we found that the dimerization of MRG chromodomains is conserved in green plants. Our findings may provide new insights into the mechanism of MRGs in regulation of gene expression in green plants.

Key words: MRG701; chromodomain; homodimer

Cite this article

Yanchao Liu , Hong Wu , Yu Yu , Ying Huang . Structural studies on MRG701 chromodomain reveal a novel dimerization interface of MRG proteins in green plants[J]. Protein & Cell, 2016 , 7(11) : 792 -803 . DOI: 10.1007/s13238-016-0310-5

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