Epigenetic underpinnings of freeze avoidance in the goldenrod gall moth, Epiblema scudderiana

J Insect Physiol. 2021 Oct:134:104298. doi: 10.1016/j.jinsphys.2021.104298. Epub 2021 Aug 17.

Abstract

The goldenrod gall moth (Epiblema scudderiana) is a cold hardy insect that survives subzero temperatures during the winter by supercooling bodily fluids to approximately -40 °C, allowing the insect to remain unfrozen despite the freezing temperatures. This is characterized by a drastic increase of cryoprotectant glycerol along with widespread downregulation of non-essential genes and processes to conserve cellular energy. This study examined the role of epigenetic enzymes in regulating this freeze-avoidant process across a range of freezing temperatures experienced in nature. Cold and subzero temperature exposure in E. scudderiana resulted in upregulation of select DNA methyltransferase (DNMT) enzymes with concurrent decreases in DNMT activity and no change in activity of the Ten-Eleven Translocation (TET) demethylation enzyme activities. Levels of histone acetyltransferase (HAT) and histone deacetylase (HDAC) activity decreased during cold exposures. The increase in DNMT expression and concurrent decrease in HAT activity suggests a role for DNA methylation to assist with transcriptional suppression. These findings propose that epigenetic regulation of genes and histones underpin the winter survival strategies of this insect.

Keywords: Cold hardiness; Cryoprotection; DNA methylation; Histone acetylation; Metabolic rate depression.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acclimatization / physiology*
  • Animals
  • Cold-Shock Response*
  • Cryoprotective Agents / metabolism
  • DNA Methylation
  • DNA-Binding Proteins / metabolism
  • Epigenesis, Genetic*
  • Freezing
  • Glycerol / metabolism
  • Histone Acetyltransferases / metabolism
  • Insect Proteins / metabolism
  • Larva / genetics
  • Larva / physiology
  • Methyltransferases / metabolism
  • Moths* / genetics
  • Moths* / physiology

Substances

  • Cryoprotective Agents
  • DNA-Binding Proteins
  • Insect Proteins
  • Methyltransferases
  • Histone Acetyltransferases
  • Glycerol