Date of Award
Master of Science
Dr. Priti Krishna
Heat shock protein 90 (Hsp90) is a highly essential molecular chaperone that regulates the maturation and activity of its client proteins. Our goal was to analyse the potential role of Hsp90 in ethylene pathway by characterizing its interaction with Ethylene Sensor 2 (ERS2), whose function is perception and transduction of ethylene in Arabidopsis thaliana. Here, we identified ERS2 as a client protein and characterized the Hsp90-ERS2 interaction using yeast two-hybrid and Bimolecular Fluorescence Complementation approaches. Based on our findings, ERS2 interacts with Hsp90 via its kinase domain and Hsp90 regulates the stability of ERS2. These data will expand our knowledge of Hsp90 function in regulating ethylene signalling as one of the important plant growth regulators, due to its role in fruit ripening and stress response. The ability to manipulate ethylene signaling in plants is important for the possible downstream applications of this finding.
Khodai-Kalaki, Maryam, "Ethylene Receptor ERS2: a New Client Protein of Hsp90 in Arabidopsis thaliana" (2011). Digitized Theses. 3379.