Coordinated maintenance of H3K36/K27 methylation by histone demethylases preserves germ cell identity and immortality

Cell Rep. 2021 Nov 23;37(8):110050. doi: 10.1016/j.celrep.2021.110050.


Germ cells have evolved unique mechanisms to ensure the transmission of genetically and nongenetically encoded information, whose alteration compromises germ cell immortality. Chromatin factors play fundamental roles in these mechanisms. H3K36 and H3K27 methyltransferases shape and propagate a pattern of histone methylation essential for C. elegans germ cell maintenance, but the role of respective histone demethylases remains unexplored. Here, we show that jmjd-5 regulates H3K36me2 and H3K27me3 levels, preserves germline immortality, and protects germ cell identity by controlling gene expression. The transcriptional and biological effects of jmjd-5 loss can be hindered by the removal of H3K27demethylases, indicating that H3K36/K27 demethylases act in a transcriptional framework and promote the balance between H3K36 and H3K27 methylation required for germ cell immortality. Furthermore, we find that in wild-type, but not in jmjd-5 mutants, alterations of H3K36 methylation and transcription occur at high temperature, suggesting a role for jmjd-5 in adaptation to environmental changes.

Keywords: H3K27 methylation; H3K36 methylation; germ cell identity; germ cell immortality; histone demethylases; temperature.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Caenorhabditis elegans / metabolism
  • Caenorhabditis elegans Proteins / metabolism
  • Chromatin / metabolism
  • Germ Cells / metabolism*
  • Histone Demethylases / metabolism*
  • Histone-Lysine N-Methyltransferase / metabolism
  • Histones / metabolism
  • Jumonji Domain-Containing Histone Demethylases / metabolism
  • Methylation


  • Caenorhabditis elegans Proteins
  • Chromatin
  • Histones
  • Histone Demethylases
  • Jumonji Domain-Containing Histone Demethylases
  • Histone-Lysine N-Methyltransferase