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Trends Biochem Sci. 2008 Apr;33(4):181-9. doi: 10.1016/j.tibs.2008.01.003. Epub 2008 Mar 17.

LSD1: oxidative chemistry for multifaceted functions in chromatin regulation.

Author information

1
Dipartimento di Genetica e Microbiologia, Università di Pavia, Via Ferrata 1, Pavia, Italy.

Abstract

Three years after its discovery, lysine-specific demethylase 1 remains at the forefront of chromatin research. Its demethylase activity on Lys4 of histone H3 supports its role in gene repression. By contrast, the biochemical mechanisms underlying lysine-specific demethylase 1 involvement in transcriptional activation are not firmly established. Structural studies highlight a specific binding site for the histone H3 N-terminal tail and a catalytic machinery that is closely related to that of other flavin-dependent amine oxidases. These insights are crucial for the development of demethylation inhibitors. Furthermore, the exploration of putative non-histone substrates and potential signaling roles of hydrogen peroxide produced by the demethylation reaction could lead to new paradigms in chromatin biology.

PMID:
18343668
DOI:
10.1016/j.tibs.2008.01.003
[Indexed for MEDLINE]

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