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Methylation: lost in hydroxylation?

Open access
Trewick, Sarah C., McLaughlin, Paul J., Allshire, Robin C.·2005·EMBO reports

Abstract

Methylation of histone tails is a key determinant in forming active and silent states of chromatin. Histone methylation was regarded as irreversible until the recent identification of a lysine‐specific histone demethylase (LSD1), which acts specifically on mono‐ and dimethylated histone H3 lysine 4. Here, we propose that the fission yeast protein Epe1 is a putative histone demethylase that could act by oxidative demethylation. Epe1 modulates the stability of silent chromatin and contains a JmjC domain. The Epe1 protein can be modelled onto the structure of the 2‐oxoglutarate‐Fe(II)‐dependent dioxygenase, factor inhibiting hypoxia inducible factor (FIH), which is a protein hydroxylase that also contains a JmjC domain. Thus, Epe1 and certain other chromatin‐associated JmjC‐domain proteins may be protein hydroxylases that catalyse a novel histone modification. Another intriguing possibility is that, by hydroxylating the methyl groups, Epe1 and certain other JmjC‐domain proteins may be able to demethylate mono‐, di‐ or trimethylated histones.

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Metadata

Authors
Trewick, S. C., McLaughlin, P. J., & Allshire, R. C.
Venue
EMBO reports
Published
2005-04
Volume
6
Issue
4
Pages
315-320
ISSN
  • 1469-221X (ISSN-L)
  • 1469-3178
OpenAlex
W1966554737
Cited by
205
References
2
FWCI
9.33
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Methylation: lost in hydroxylation? https://app.cochat.ai/papers/10.1038/sj.embor.7400379
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Trewick, S. C., McLaughlin, P. J., & Allshire, R. C. (2005). Methylation: lost in hydroxylation? EMBO reports. https://doi.org/10.1038/sj.embor.7400379

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