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Submitted to: Meeting Abstract
Publication Type: Abstract Only Publication Acceptance Date: 7/31/2007 Publication Date: 8/19/2007 Citation: Rinehart, J.P. 2007. Heat shock proteins and diapause: How downstream gene expression can affect diapause success. Proceedings of International Congress of Insect Biotechnology and Industry. Entomological Research 37(Suppl. 1):A18-A19. Interpretive Summary: Technical Abstract: Many of the physiological and molecular studies of diapause have focused on how diapause is controlled. Clearly, these are fascinating questions, and deciphering the molecular pathways that both initiate and terminate diapause will give us a deeper understanding of how many important processes are controlled and will provide greater opportunities for both insect control and insect storage. However, investigating the downstream components of diapause is not without merit. Nearly ten years ago, we first reported that a member of the small heat shock protein family was expressed in high levels in diapausing flesh fly pupae in the absence of stress. Since that time, many more heat shock proteins have been found to be upregulated during flesh fly diapause. And while not universal, similar observations have been made for the diapause of many other species representing a wide range of insect orders and during a variety of life stages. One question remained at the end of these studies: what role do these genes play during diapause? Is their upregulation a key regulatory event in the diapause program, or is it just another molecular curiosity during this fascinating suspension of development? Using RNAi, we have found that while neither diapause induction nor diapause duration is affected when these genes are suppressed, diapause-associated cold tolerance is substantially diminished. Hence, even though the upregulation of hsps does not appear to be an essential component of the molecular pathways controlling diapause, it can be essential for successful diapause in temperate environments. |
