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Background
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LSD1 is a histone demethylase that specifically demethylates 'Lys-4' of histone H3, a specific tag for epigenetic transcriptional activation, thereby acting as a corepressor. LSD1 contains a SWIRM domain, a FAD-binding motif, and an amine oxidase domain. This protein is a component of several histone deacetylase complexes, though it silences genes by functioning as a histone demethylase. It acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. LSD1 demethylates both mono- and tri-methylted 'Lys-4' of histone H3. This protein may play a role in the repression of neuronal genes. Alone, it is unable to demethylate H3 'Lys-4' on nucleosomes and requires the presence of RCOR1/CoREST to achieve such activity. It may also demethylate 'Lys-9' of histone H3, a specific tag for epigenetic transcriptional repression, thereby leading to derepression of androgen receptor target genes.
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Background
References
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- Forneris,F., et al. FEBS Lett. 579 (10), 2203-2207 (2005)
- Shi,Y., et al. Cell 119 (7), 941-953 (2004)
- Hakimi,M.A., et al. J. Biol. Chem. 278 (9), 7234-7239 (2003)
- Hakimi,M.A., et al. PNAS 99 (11), 7420-7425 (2002)
- Humphrey,G.W., et al. J. Biol. Chem. 276 (9), 6817-6824 (2001)
- Ota, T., et al., Nat. Genet. 36(1):40-45 (2004).
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