Poster: Signaling, long distance

Abs # 460: Hsp90 and ethylene: is there a connection?

Presenter:	Krishna, Priti , pkrishna@uwo.ca
Authors	Wang, Zezhou  (A)   Zhang, Zhongming  (A)   Krishna, Priti  (A)
Affiliations:	(A): University Of Western Ontario

The highly conserved and abundant molecular chaperone hsp90 plays a key role in signal transduction networks, cell-cycle control, protein degradation and protein trafficking. A critical dependence on hsp90 has been established for animal steroid hormone receptors and several serine/threonine and tyrosine kinases. The number of identified client proteins whose functions are facilitated by hsp90 continues to grow in animal systems. Though the hsp90 protein family is largest in plants, the client proteins of plant hsp90, for the most part, remain unidentified. We are using a broad proteomics-based approach to identify hsp90 interactors. Of the several positive clones identified in a yeast two-hybrid screen, we have confirmed the interaction of hsp90 with two members of the ethylene receptor family and two novel proteins containing tetratricopeptide repeat domain. These results will be discussed in the context of the hsp90 chaperone system in plants, and of the potential roles of hsp90 in the ethylene signaling pathway.