Submitted to: International Congress of Nematology
Publication Type: Abstract Only
Publication Acceptance Date: June 8, 2002
Publication Date: June 8, 2002
Citation: Skantar, A.M., Agama, K.K., Carta, L.K. 2002. Functional analysis of heat shock protein HSP90, from the soybean cyst nematode, Heterodera glycines [Abstract]. Nematology. 4(2):180. Technical Abstract: Developmentally arrested second-stage juveniles of many plant parasites are functionally similar to Caenorhabditis elegans dauers, and likely use molecules similar to those defined by the C. elegans dauer pathway to regulate developmental arrest, lifespan, and chemosensation. One C. elegans dauer pathway gene, daf-21, encodes an HSP90 molecular chaperone. The precise function of daf-21 is unclear; however, HSP90 chaperones are known to refold denatured or misfolded proteins, especially under conditions of stress. In many systems, HSP90 guides the proper folding of specific target proteins, including nuclear hormone receptors and protein kinases. We are currently examining the effect of an HSP90 inhibitor, geldanamycin, on C. elegans development. Disruption of normal development by this compound would implicate a role for HSP90 in this process, and form the basis for similar studies in plant-parasitic nematodes. We have also initiated a yeast two hybrid screen using Heterodera glycines HSP90 as bait, to identify co-chaperones or target proteins, some of which may include dauer pathway homologs that are critical to plant-parasitic nematode development. In the absence of robust transformation or RNAi strategies for plant-parasitic nematodes, the yeast two hybrid approach should provide a tractable system for analyzing gene function and identifying critical protein-protein interactions.