Abstract

As sessile organisms, plants are unable to escape environmental stressors that they may be faced with. As a result, they have developed a unique stress detection and response system involving calcium signals. These signals are received by calcium binding proteins, which are able to alter the gene expression, or metabolic activity of the cell. Calmodulin (CaM) is one of the primary calcium binding proteins. In addition to CaM, plants have evolved a family of calmodulin-like proteins (CMLs) that also function in calcium signaling. One particular CML, CML43, has been found to be linked with bacterial and viral pathogen detection and response in a few species of plants, including Arabidopsis thaliana and tomato. This study attempted to discover the protein targets of CML43 during calcium signaling, and its role in stress recognition and response. Yeast two hybrid analysis was found to be the best method for this particular kind of study because it allows for a high-throughput method of determining protein-protein interactions. Many putative interactors were found, and results from the purification and sequences of these interactors will be presented.

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