Abstract
Environmental stresses such as low temperature have significant impact on various metabolic activities in chloroplasts. Cold stress also leads to the injury of membranes and the inactivation of proteins. Under low temperature stress, plants accumulate COR (cold-regulated) proteins targeted to chloroplasts, which may protect chloroplasts from dysfunction. However, biochemical functions of these proteins remain to be determined. Here, we report biochemical analysis of Arabidopsis thaliana Cor15a protein. As a first step of our analysis, we produced the Cor15a-His recombinant protein in E. coli and generated antibody against Cor15a. Using this antibody, we examined the expression, localization and immunoaffinity purification of Cor15a. To purify the Cor15a complex, we also generated Arabidopsis overexpressing COR15a-PROTEIN A fusion construct by Agrobacterium-mediated transformation. We show the analysis of these plants and discuss biochemical and physiological roles of Cor15a under cold stress.
