The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.
A Novel Mammalian Flavin-dependent Histone Demethylase
Open accessAbstract
Methylation of Lys residues on histone proteins is a well known and extensively characterized epigenetic mark. The recent discovery of lysine-specific demethylase 1 (LSD1) demonstrated that lysine methylation can be dynamically controlled. Among the histone demethylases so far identified, LSD1 has the unique feature of functioning through a flavin-dependent amine oxidation reaction. Data base analysis reveals that mammalian genomes contain a gene (AOF1, for amine-oxidase flavin-containing domain 1) that is homologous to the LSD1-coding gene. Here, we demonstrate that the protein encoded by AOF1 represents a second mammalian flavin-dependent histone demethylase, named LSD2. The new demethylase is strictly specific for mono- and dimethylated Lys4 of histone H3, recognizes a long stretch of the H3 N-terminal tail, senses the presence of additional epigenetic marks on the histone substrate, and is covalently inhibited by tranylcypromine. As opposed to LSD1, LSD2 does not form a biochemically stable complex with the C-terminal domain of the corepressor protein CoREST. Furthermore, LSD2 contains a CW-type zinc finger motif with potential zinc-binding sites that are not present in LSD1. We conclude that mammalian LSD2 represents a new flavin-dependent H3-Lys4 demethylase that features substrate specificity properties highly similar to those of LSD1 but is very likely to be part of chromatin-remodeling complexes that are distinct from those involving LSD1.
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Cites
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Mosammaparast, N., & Shi, Y. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.070907.103946 · Cited by 585
Interplay between Metabolism and Epigenetics: A Nuclear Adaptation to Environmental Changes
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Metadata
- Authors
- Karytinos, A., Forneris, F., Profumo, A., Ciossani, G., Battaglioli, E., Binda, C., & Mattevi, A.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2009-06
- Volume
- 284
- Issue
- 26
- Pages
- 17775-17782
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2064887977
- Cited by
- 273
- References
- 33
- FWCI
- 7.44
- Type
- journal article
- Language
- en
- Open access
- hybrid
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