Understanding the language of Lys36 methylation at histone H3

Eric Wagner, Phillip B. Carpenter

Research output: Contribution to journalArticle

396 Citations (Scopus)

Abstract

Histone side chains are post-translationally modified at multiple sites, including at Lys36 on histone H3 (H3K36). Several enzymes from yeast and humans, including the methyltransferases SET domain-containing 2 (Set2) and nuclear receptor SET domain-containing 1 (NSD1), respectively, alter the methylation status of H3K36, and significant progress has been made in understanding how they affect chromatin structure and function. Although H3K36 methylation is most commonly associated with the transcription of active euchromatin, it has also been implicated in diverse processes, including alternative splicing, dosage compensation and transcriptional repression, as well as DNA repair and recombination. Disrupted placement of methylated H3K36 within the chromatin landscape can lead to a range of human diseases, underscoring the importance of this modification.

Original languageEnglish (US)
Pages (from-to)115-126
Number of pages12
JournalNature Reviews Molecular Cell Biology
Volume13
Issue number2
DOIs
StatePublished - Feb 2012
Externally publishedYes

Fingerprint

Histones
Methylation
Chromatin
Language
Euchromatin
Alternative Splicing
Methyltransferases
Cytoplasmic and Nuclear Receptors
DNA Repair
Genetic Recombination
Yeasts
Enzymes

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

Cite this

Understanding the language of Lys36 methylation at histone H3. / Wagner, Eric; Carpenter, Phillip B.

In: Nature Reviews Molecular Cell Biology, Vol. 13, No. 2, 02.2012, p. 115-126.

Research output: Contribution to journalArticle

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