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Author Notes:
Correspondence: Xiaodong Cheng; Phone: 404-727-8491; Fax: 404-727-3746; Email: xcheng@emory.edu
Acknowledgments: We thank Dr. Hideharu Hashimoto for discussion on PHF2 and making figure 5b; Ruogu (Roc) Hu for making figure 5a, and Dr. Marc A. Bailly for reading the manuscript.
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Research Funding:
The work in the Cheng laboratory was supported by grants GM068680 and GM049245 from the National Institutes of Health.
X.C. is a Georgia Research Alliance Eminent Scholar.
Coordinated Methyl-lysine Erasure: Structural and Functional Linkage of a Jumonji demethylasedomain and a Reader domain
Abstract:
Both components of chromatin (DNA and histones) are subjected to dynamic post-synthetic covalent modifications. Dynamic histone lysine methylation involves the activities of modifying enzymes (writers), enzymes removing modifications (erasers), and readers of the epigenetic code. Known histone lysine demethylases include flavin-dependent monoamine oxidase LSD1 and α-ketoglutarate-Fe(II)-dependent dioxygenases containing Jumonji domains. Importantly, the Jumonji domain often associates with at least one additional recognizable domain (reader) within the same polypeptide that detects the methylation status of histones and/or DNA. Here, we summarize recent developments in characterizing structural and functional properties of various histone lysine demethylases, with emphasis on a mechanism of crosstalk between a Jumonji domain and its associated reader module(s). We further discuss the role of recently identified Tet1 enzyme in oxidizing 5-methylcytosine to 5-hydroxymethylcytosine in DNA.
Copyright information:
© 2011 Elsevier Ltd. All rights reserved.
This is an Open Access work distributed under the terms of the Creative Commons Attribution-NonCommerical-NoDerivs 3.0 Unported License (http://creativecommons.org/licenses/by-nc-nd/3.0/).
