PUBLICATION

Histone deacetylase activity mediates thermal plasticity in zebrafish (Danio rerio)

Authors
Seebacher, F., Simmonds, A.I.M.
ID
ZDB-PUB-190605-7
Date
2019
Source
Scientific Reports   9: 8216 (Journal)
Registered Authors
Keywords
none
MeSH Terms
  • Acclimatization/physiology*
  • Adenylate Kinase/metabolism
  • Animals
  • Atropine/pharmacology
  • Heart Rate/physiology
  • Histone Deacetylases/metabolism*
  • Hydroxamic Acids/pharmacology
  • Isoproterenol/pharmacology
  • Metabolomics
  • Muscle Proteins/metabolism
  • Muscle, Skeletal/drug effects
  • Muscle, Skeletal/metabolism
  • Myocardium/metabolism
  • Myosin Heavy Chains/metabolism
  • Sarcoplasmic Reticulum Calcium-Transporting ATPases/metabolism
  • Stroke Volume/drug effects
  • Swimming
  • Temperature*
  • Zebrafish/metabolism
  • Zebrafish/physiology*
PubMed
31160672 Full text @ Sci. Rep.
Abstract
Regulatory mechanisms underlying thermal plasticity determine its evolution and potential to confer resilience to climate change. Here we show that class I and II histone deacetylases (HDAC) mediated thermal plasticity globally by shifting metabolomic profiles of cold acclimated zebrafish (Danio rerio) away from warm acclimated animals. HDAC activity promoted swimming performance, but reduced slow and fast myosin heavy chain content in cardiac and skeletal muscle. HDAC increased sarco-endoplasmic reticulum ATPase activity in cold-acclimated fish but not in warm-acclimated animals, and it promoted cardiac function (heart rate and relative stroke volume) in cold but not in warm-acclimated animals. HDAC are an evolutionarily ancient group of proteins, and our data show that they mediate the capacity for thermal plasticity, although the actual manifestation of plasticity is likely to be determined by interactions with other regulators such as AMP-activated protein kinase and thyroid hormone.
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Mapping