Research Projects

Being sessile, plants need to constantly deal with the ever-changing external environment in which they grow. Several factors, including abiotic stresses, especially high temperature is known to trigger protein misfolding and aggregation in cells. While misfolding and aggregation often causes proteins to become non-functional or cytotoxic, reports also indicate that some protein aggregates may work as epigenetic regulators of myriad cellular processes. Thereby, some protein aggregates have the potential to affect the morphology or physiology of organisms under normal as well as stress conditions. All organisms are equipped with an intricate network of molecular chaperones to deal with aggregation of proteins. Different chaperone families, like the small Hsps, J-domain proteins (JDPs), Hsp70 and Hsp100 have a profound effect on the propensity of aggregation as well as remodelling of such aggregates in cells. While such aggregate prone proteins are ubiquitous, they are lesser studied in plants. Studying aggregation-prone proteins in plants and the effects of molecular chaperones over them will help unravel how chaperones can modulate their aggregate dynamics to affect plant growth and development, stress-tolerance, morphology or behaviour. Here we aim to identify and characterize aggregate prone proteins from Arabidopsis and study how chaperones affect their aggregation or solubilization, thus epigenetically affecting plant growth and development. This study has significant translational and academic value which will potentiate new investigations on protein aggregation associated phenotypes in plants and role of chaperones in modulating them.