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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
Author(s) -
Sonoda Shoji,
Fukumoto Katsue,
Izumi Yohei,
Yoshida Hideya,
Tsumuki Hisaaki
Publication year - 2006
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.20138
Subject(s) - chilo suppressalis , biology , diapause , manduca sexta , heat shock protein , complementary dna , amino acid , microbiology and biotechnology , hsp90 , botany , biochemistry , insect , larva , gene
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 suppressalis 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. Arch Insect Biochem Physiol 63:36–47, 2006. © 2006 Wiley‐Liss, Inc.