TY - JOUR
T1 - Coordinated methyl-lysine erasure
T2 - Structural and functional linkage of a Jumonji demethylase domain and a reader domain
AU - Upadhyay, Anup K.
AU - Horton, John R.
AU - Zhang, Xing
AU - Cheng, Xiaodong
N1 - Funding Information:
We thank Dr Hideharu Hashimoto for discussion on PHF2 and making Figure 5 b; Ruogu (Roc) Hu for making Figure 5 a, and Dr Marc A. Bailly for reading the manuscript. 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.
PY - 2011/12
Y1 - 2011/12
N2 - Both components of chromatin (DNA and histones) are subjected to dynamic postsynthetic 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 lysine-specific demethylase 1 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.
AB - Both components of chromatin (DNA and histones) are subjected to dynamic postsynthetic 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 lysine-specific demethylase 1 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.
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U2 - 10.1016/j.sbi.2011.08.003
DO - 10.1016/j.sbi.2011.08.003
M3 - Review article
C2 - 21872465
AN - SCOPUS:82955195630
SN - 0959-440X
VL - 21
SP - 750
EP - 760
JO - Current Opinion in Structural Biology
JF - Current Opinion in Structural Biology
IS - 6
ER -