Structure and function of histone methylation-binding proteins in plants.
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.
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 yanliliu@mail.ccnu.edu.cn.
Yanli
Y
Liu
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.
Jinrong
J
Min
D029681:Arabidopsis Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D006657:Histones / Q000378:metabolism*; D008745:Methylation; D010940:Plant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D010944:Plants / Q000378:metabolism*; D011499:Protein Processing, Post-Translational
D029681:Arabidopsis Proteins; D006657:Histones; D010940:Plant Proteins
epigenetics; histone methylation readers; histone post-translational modifications