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Heat‐shock protein 90 is down‐regulated during pupal diapause in the flesh fly, Sarcophaga crassipalpis , but remains responsive to thermal stress
Author(s) -
Rinehart Joseph P.,
Denlinger David L.
Publication year - 2000
Publication title -
insect molecular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.955
H-Index - 93
eISSN - 1365-2583
pISSN - 0962-1075
DOI - 10.1046/j.1365-2583.2000.00230.x
Subject(s) - flesh fly , diapause , biology , pupa , heat shock protein , flesh , shock (circulatory) , microbiology and biotechnology , horticulture , botany , medicine , biochemistry , gene , larva
Heat‐shock protein 23 (hsp23) and hsp70 are both known to be strongly up‐regulated during pupal diapause in the flesh fly Sarcophaga crassipalpis . This prompted us to investigate whether hsp90 was also up‐regulated during diapause. To test this possibility, we developed a partial clone of a hsp90 family member for use as a probe in Northern blot hybridization. Both high and low temperature exposure up‐regulated hsp90 transcripts in nondiapausing individuals. In contrast to hsp23 and hsp70 , hsp90 was down‐regulated following entry into diapause, and returned to prediapause levels after diapause termination. The response of hsp90 to heat shock and cold shock remained intact during diapause: both shocks evoked elevated expression. The results indicate differential regulation of hsps during diapause and in response to thermal injury inflicted on diapausing pupae.