Cloning of heat shock protein genes (hsp90 and hsc70) and their expression during larval diapause and cold tolerance acquisition in the rice stem borer, Chilo suppressalis walker

Shoji Sonoda, Katsue Fukumoto, Yohei Izumi, Hideya Yoshida, Hisaaki Tsumuki

Research output: Contribution to journalArticle

80 Citations (Scopus)


The complete cDNA sequences of heat shock protein 90 (hsp90) and of heat shock cognate protein 70 (hsc70) were cloned by reverse transcription polymerase chain reaction from the rice stem borer, Chilo suppressed Walker. They potentially encode a 717-amino-acids (hsp90) and a 652-amino-acids (hsc70) protein, with calculated molecular weight of 82.5 and 71.3 kDa, respectively. The deduced amino acid sequence of hsp90 showed the highest homology of 97.2% to Spodoptera frugiperda hsp90. The closest match of C. suppressalis hsc70 was with Manduca sexta hsc70 at 98.0% identity. Expression of hsp90 in diapausing larvae was higher than that in non-diapausing larvae. No such up-regulation in diapausing larvae was observed for hsc70. In non-diapausing larvae, but not in diapausing ones, hsp90 expression was up-regulated by cold acclimation. Hsc70 expression slightly decreased during cold acclimation irrespective of the state of diapause. Involvement of hsp90 and hsc70 in larval diapause and cold tolerance acquisition in C. suppressalis is discussed.

Original languageEnglish
Pages (from-to)36-47
Number of pages12
JournalArchives of Insect Biochemistry and Physiology
Issue number1
Publication statusPublished - Sep 2006
Externally publishedYes



  • Chilo suppressalis
  • Cold tolerance
  • Diapause
  • Heat shock protein
  • Rice stem borer

ASJC Scopus subject areas

  • Insect Science
  • Biochemistry, Genetics and Molecular Biology(all)
  • Physiology
  • Physiology (medical)

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