Post-translational modifications of histones play important roles in modulating many essential biological processes in both animals and plants. These covalent modifications, including methylation, acetylation, phosphorylation, ubiquitination, SUMOylation and so on, are laid out and erased by histone-modifying enzymes and read out by effector proteins. Recent studies have revealed that a number of developmental processes in plants are under the control of histone post-translational modifications, such as floral transition, seed germination, organogenesis and morphogenesis. Therefore, it is critical to identify those protein domains, which could specifically recognize these post-translational modifications to modulate chromatin structure and regulate gene expression. In the present review, we discuss the recent progress in understanding the structure and function of the histone methylation readers in plants, by focusing on Arabidopsis thaliana proteins.
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June 2016
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K-Ras4B membrane-anchored dimers in the cell. Dimerization can take place through helical (left) and beta-sheet (right) interfaces. The major (front) and minor (back) conformations are shown. For further details please see pp. 1719–1732. Image kindly provided by Ruth Nussinov. - PDF Icon PDF LinkFront Matter
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Review Article|
June 10 2016
Structure and function of histone methylation-binding proteins in plants
Yanli Liu;
Yanli Liu
1
*Hubei Key Laboratory of Genetic Regulation and Integrative Biology, College of Life Science, Central China Normal University, Wuhan 430079, PR China
†Structural Genomics Consortium, University of Toronto, 101 College Street, Toronto, Ontario, Canada, M5G 1L7
1To whom correspondence should be addressed (email yanliliu@mail.ccnu.edu.cn).
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Jinrong Min
Jinrong Min
*Hubei Key Laboratory of Genetic Regulation and Integrative Biology, College of Life Science, Central China Normal University, Wuhan 430079, PR China
†Structural Genomics Consortium, University of Toronto, 101 College Street, Toronto, Ontario, Canada, M5G 1L7
‡Department of Physiology, University of Toronto, Toronto, Ontario, Canada, M5S 1A8
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Publisher: Portland Press Ltd
Received:
December 21 2015
Revision Received:
February 17 2016
Accepted:
February 29 2016
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© 2016 The Author(s). published by Portland Press Limited on behalf of the Biochemical Society
2016
Biochem J (2016) 473 (12): 1663–1680.
Article history
Received:
December 21 2015
Revision Received:
February 17 2016
Accepted:
February 29 2016
Citation
Yanli Liu, Jinrong Min; Structure and function of histone methylation-binding proteins in plants. Biochem J 15 June 2016; 473 (12): 1663–1680. doi: https://doi.org/10.1042/BCJ20160123
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