A chitinase structurally related to the glycoside hydrolase family 48 is indispensable for the hormonally induced diapause termination in a beetle

Biochem Biophys Res Commun. 2006 Jun 23;345(1):502-7. doi: 10.1016/j.bbrc.2006.04.126. Epub 2006 May 2.

Abstract

Two proteins (APAP I and II) of the glycoside hydrolase family 48 (Family GH48) were isolated from the active adults of the leaf beetle Gastrophysa atrocyanea. Full-length and cDNAs were sequenced. APAP I expression and function were examined in detail. The protein has a chitinase but not a glucanase and cellobiohydrolase activity. It is expressed in the feeding stages, including beetles whose diapause was terminated with a juvenile hormone agonist. Suppression of the APAP I expression by means of RNA interference prevented the hormonal termination of diapause.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Chitinases / metabolism*
  • Coleoptera / drug effects
  • Coleoptera / physiology*
  • Feeding Behavior / drug effects
  • Feeding Behavior / physiology*
  • Glycoside Hydrolases / metabolism*
  • Isoenzymes / metabolism
  • Juvenile Hormones / pharmacology*
  • Life Cycle Stages / drug effects
  • Life Cycle Stages / physiology*

Substances

  • Isoenzymes
  • Juvenile Hormones
  • Glycoside Hydrolases
  • Chitinases