Heat-shock protein 90 is down-regulated during pupal diapause in the flesh fly, Sarcophaga crassipalpis, but remains responsive to thermal stress.
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.
Rinehart
J P
JP
Department of Entomology, Ohio State University, Columbus, OH 43210, USA.
Denlinger
D L
DL
D000595:Amino Acid Sequence; D000818:Animals; D015152:Blotting, Northern; D004175:Diptera / Q000235:genetics*; D015536:Down-Regulation; D017344:Genes, Insect; D018841:HSP90 Heat-Shock Proteins / Q000235:genetics*; D018869:Heat-Shock Response; D008969:Molecular Sequence Data; D011679:Pupa; D020133:Reverse Transcriptase Polymerase Chain Reaction; D017386:Sequence Homology, Amino Acid
D018841:HSP90 Heat-Shock Proteins