TY - JOUR
T1 - Structural insights into histone lysine demethylation
AU - Hou, Haifeng
AU - Yu, Hongtao
N1 - Funding Information:
Research in our laboratory is supported by the National Institutes of Health and the Welch Foundation (I-1441). H.Y. is an Investigator at the Howard Hughes Medical Institute.
PY - 2010/12
Y1 - 2010/12
N2 - Posttranslational modifications of histone tails are crucial epigenetic marks that regulate diverse cellular processes. Histone lysine methylation activates or represses transcription, depending on the site and degree of these modifications. Two classes of histone lysine demethylases remove histone methylation. Lysine demethylase 1 (KDM1, also known as LSD1) is a flavin adenine dinucleotide (FAD)-containing enzyme that removes mono-/di-methylation. The Jumonji C-terminal domain (JmjC) family of histone demethylases uses Fe2+ and α-ketoglutarate as cofactors to remove all methylation states. Structural studies have provided insights into the overall architecture, the catalytic mechanism, and the substrate specificity of histone demethylases. Here, we review these exciting advances in the structure biology of histone demethylases and discuss the general principles applicable to other histone-modifying enzymes.
AB - Posttranslational modifications of histone tails are crucial epigenetic marks that regulate diverse cellular processes. Histone lysine methylation activates or represses transcription, depending on the site and degree of these modifications. Two classes of histone lysine demethylases remove histone methylation. Lysine demethylase 1 (KDM1, also known as LSD1) is a flavin adenine dinucleotide (FAD)-containing enzyme that removes mono-/di-methylation. The Jumonji C-terminal domain (JmjC) family of histone demethylases uses Fe2+ and α-ketoglutarate as cofactors to remove all methylation states. Structural studies have provided insights into the overall architecture, the catalytic mechanism, and the substrate specificity of histone demethylases. Here, we review these exciting advances in the structure biology of histone demethylases and discuss the general principles applicable to other histone-modifying enzymes.
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U2 - 10.1016/j.sbi.2010.09.006
DO - 10.1016/j.sbi.2010.09.006
M3 - Review article
C2 - 20970991
AN - SCOPUS:78649664485
SN - 0959-440X
VL - 20
SP - 739
EP - 748
JO - Current Opinion in Structural Biology
JF - Current Opinion in Structural Biology
IS - 6
ER -