Repressive Chromatin in Caenorhabditis elegans: Establishment, Composition, and Function

Genetics. 2018 Feb;208(2):491-511. doi: 10.1534/genetics.117.300386.

Abstract

Chromatin is organized and compacted in the nucleus through the association of histones and other proteins, which together control genomic activity. Two broad types of chromatin can be distinguished: euchromatin, which is generally transcriptionally active, and heterochromatin, which is repressed. Here we examine the current state of our understanding of repressed chromatin in Caenorhabditis elegans, focusing on roles of histone modifications associated with repression, such as methylation of histone H3 lysine 9 (H3K9me2/3) or the Polycomb Repressive Complex 2 (MES-2/3/6)-deposited modification H3K27me3, and on proteins that recognize these modifications. Proteins involved in chromatin repression are important for development, and have demonstrated roles in nuclear organization, repetitive element silencing, genome integrity, and the regulation of euchromatin. Additionally, chromatin factors participate in repression with small RNA pathways. Recent findings shed light on heterochromatin function and regulation in C. elegans, and should inform our understanding of repressed chromatin in other animals.

Keywords: C. elegans; H3K27me; H3K9me; WormBook; chromatin; heterochromatin; histone methylation.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Caenorhabditis elegans / genetics*
  • Caenorhabditis elegans / metabolism
  • Cellular Reprogramming / genetics
  • Chromatin / genetics*
  • Chromatin / metabolism
  • Gene Expression Regulation
  • Genome
  • Heterochromatin / genetics
  • Heterochromatin / metabolism
  • Histone Code
  • Histone-Lysine N-Methyltransferase / metabolism
  • Histones / metabolism
  • Loss of Function Mutation
  • Methylation
  • Nuclear Lamina / metabolism
  • Phenotype
  • RNA Interference
  • Repetitive Sequences, Nucleic Acid

Substances

  • Chromatin
  • Heterochromatin
  • Histones
  • Histone-Lysine N-Methyltransferase