Histone H3 trimethylation at lysine 36 is associated with constitutive and facultative heterochromatin

Sophie Chantalat, Arnaud Depaux, Patrick Héry, Sophie Barral, Jean Yves Thuret, Stefan Dimitrov, Matthieu Gérard

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Abstract

The mammalian genome contains numerous regions known as facultative heterochromatin, which contribute to transcriptional silencing during development and cell differentiation. We have analyzed the pattern of histone modifications associated with facultative heterochromatin within the mouse imprinted Snurf-Snrpn cluster, which is homologous to the human Prader-Willi syndrome genomic region. We show here that the maternally inherited Snurf-Snrpn 3-Mb region, which is silenced by a potent transcription repressive mechanism, is uniformly enriched in histone methylation marks usually found in constitutive heterochromatin, such as H4K20me3, H3K9me3, and H3K79me3. Strikingly, we found that trimethylated histone H3 at lysine 36 (H3K36me3), which was previously identified as a hallmark of actively transcribed regions, is deposited onto the silenced, maternally contributed 3-Mb imprinted region. We show that H3K36me3 deposition within this large heterochromatin domain does not correlate with transcription events, suggesting the existence of an alternative pathway for the deposition of this histone modification. In addition, we demonstrate that H3K36me3 is markedly enriched at the level of pericentromeric heterochromatin in mouse embryonic stem cells and fibroblasts. This result indicates that H3K36me3 is associated with both facultative and constitutive heterochromatin. Our data suggest that H3K36me3 function is not restricted to actively transcribed regions only and may contribute to the composition of heterochromatin, in combination with other histone modifications.

Original languageEnglish
Pages (from-to)1426-1437
Number of pages12
JournalGenome Research
Volume21
Issue number9
DOIs
Publication statusPublished - Sep 2011
Externally publishedYes

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Heterochromatin
Histones
Lysine
Histone Code
Prader-Willi Syndrome
Methylation
Cell Differentiation
Fibroblasts
Genome

ASJC Scopus subject areas

  • Genetics
  • Genetics(clinical)

Cite this

Histone H3 trimethylation at lysine 36 is associated with constitutive and facultative heterochromatin. / Chantalat, Sophie; Depaux, Arnaud; Héry, Patrick; Barral, Sophie; Thuret, Jean Yves; Dimitrov, Stefan; Gérard, Matthieu.

In: Genome Research, Vol. 21, No. 9, 09.2011, p. 1426-1437.

Research output: Contribution to journalArticle

Chantalat, S, Depaux, A, Héry, P, Barral, S, Thuret, JY, Dimitrov, S & Gérard, M 2011, 'Histone H3 trimethylation at lysine 36 is associated with constitutive and facultative heterochromatin', Genome Research, vol. 21, no. 9, pp. 1426-1437. https://doi.org/10.1101/gr.118091.110
Chantalat, Sophie ; Depaux, Arnaud ; Héry, Patrick ; Barral, Sophie ; Thuret, Jean Yves ; Dimitrov, Stefan ; Gérard, Matthieu. / Histone H3 trimethylation at lysine 36 is associated with constitutive and facultative heterochromatin. In: Genome Research. 2011 ; Vol. 21, No. 9. pp. 1426-1437.
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