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| Subject Categories: Chromatin & Transcription |
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| The EMBO Journal
(2007) 26, 4670–4682, doi:10.1038/sj.emboj.7601892 Published online 18 October 2007 |
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| The JmjC domain protein Epe1 prevents unregulated assembly and disassembly of heterochromatin EMBO Open |
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| Sarah C Trewick1, Elsa Minc1, Richard Antonelli1, Takeshi Urano2 and Robin C Allshire1 |
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1 Wellcome Trust Centre for Cell Biology, The University of Edinburgh, Edinburgh, UK 2 Department of Biochemistry II, Nagoya University School of Medicine, Showa-ku, Nagoya, Japan To whom correspondence should be addressed Sarah C Trewick, Institute of Cell Biology, Wellcome Trust Centre for Cell Biology, School of Biological Sciences, The University of Edinburgh, 6.34 Swann Building, The King's Buildings, Mayfield Road, Edinburgh EH9 3JR, UK. Tel.: +44 131 650 7117; Fax: +44 845 280 2340; E-mail: strewick@staffmail.ed.ac.uk Robin C Allshire, Institute of Cell Biology, Wellcome Trust Centre for Cell Biology, School of Biological Sciences, The University of Edinburgh, 6.34 Swann Building, The King's Buildings, Mayfield Road, Edinburgh EH9 3JR, UK. Tel.: +44 131 650 7117; Fax: +44 845 280 2340; E-mail: robin.allshire@ed.ac.uk Received 20 April 2007; Accepted 18 September 2007; Published online 18 October 2007. |
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| Abstract |
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| Heterochromatin normally has prescribed chromosomal positions and must not encroach on adjacent regions. We demonstrate that the fission yeast protein Epe1 stabilises silent chromatin, preventing the oscillation of heterochromatin domains. Epe1 loss leads to two contrasting phenotypes: alleviation of silencing within heterochromatin and expansion of silent chromatin into neighbouring euchromatin. Thus, we propose that Epe1 regulates heterochromatin assembly and disassembly, thereby affecting heterochromatin integrity, centromere function and chromosome segregation fidelity. Epe1 regulates the extent of heterochromatin domains at the level of chromatin, not via the RNAi pathway. Analysis of an ectopically silenced site suggests that heterochromatin oscillation occurs in the absence of heterochromatin boundaries. Epe1 requires predicted iron- and 2-oxyglutarate (2-OG)-binding residues for in vivo function, indicating that it is probably a 2-OG/Fe(II)-dependent dioxygenase. We suggest that, rather than being a histone demethylase, Epe1 may be a protein hydroxylase that affects the stability of a heterochromatin protein, or protein–protein interaction, to regulate the extent of heterochromatin domains. Thus, Epe1 ensures that heterochromatin is restricted to the domains to which it is targeted by RNAi. |
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| Keywords: centromere, Epe1, fission yeast, heterochromatin, JmjC domain |
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