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Curr Opin Struct Biol. 2010 Dec;20(6):739-48. doi: 10.1016/j.sbi.2010.09.006. Epub 2010 Oct 21.

Structural insights into histone lysine demethylation.

Author information

1
Howard Hughes Medical Institute, Department of Pharmacology, University of Texas Southwestern Medical Center, 6001 Forest Park Road, Dallas, TX 75390, USA.

Abstract

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 Fe(2+) 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.

PMID:
20970991
PMCID:
PMC3010374
DOI:
10.1016/j.sbi.2010.09.006
[Indexed for MEDLINE]
Free PMC Article

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