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Review
. 2015;9(1):36-44.
doi: 10.1080/19336934.2015.1074787.

Histone lysine demethylases in Drosophila melanogaster

Andreana Holowatyj  1 , Zeng-Quan Yang, Lori A Pile
Affiliations
Review

Histone lysine demethylases in Drosophila melanogaster

Andreana Holowatyj et al. Fly (Austin). 2015.

Abstract

Epigenetic regulation of chromatin structure is a fundamental process for eukaryotes. Regulators include DNA methylation, microRNAs and chromatin modifications. Within the chromatin modifiers, one class of enzymes that can functionally bind and modify chromatin, through the removal of methyl marks, is the histone lysine demethylases. Here, we summarize the current findings of the 13 known histone lysine demethylases in Drosophila melanogaster, and discuss the critical role of these histone-modifying enzymes in the maintenance of genomic functions. Additionally, as histone demethylase dysregulation has been identified in cancer, we discuss the advantages for using Drosophila as a model system to study tumorigenesis.

Keywords: Drosophila; Epigenetics; JmjC domain; KDM; cancer; chromatin; demethylase; histone; modifications; tumorigenesis.

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Figures

Figure 1.
Figure 1.
Detailed structures of the 13 histone lysine demethylases in Drosophila melanogaster.
Figure 2.
Figure 2.
Mechanisms of lysine demethylation. (A) Mechanism of LSD1 demethylation via an amine oxidation reaction. (B) Mechanism of JmjC protein demethylation via a hydroxylation reaction. Adapted from Cloos et al.
See this image and copyright information in PMC

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