Conserved Oligopeptides in the Rubisco Large Chains

The evolution of intelligent behavior observed in metazoan species requires a steady and sufficient supply of energy. Photosynthesis assumes the important role in the evolutionary mechanism in this respect. Since the basic mechanism of photosynthesis has remained unchanged in the evolutionary pathway, the study of the molecular evolution of the photosynthetic proteins has gained importance. Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) catalyses the first step in the CO2 assimilation in Photosynthesis. RuBisCO exists as dimmer in case of prokaryotic autotrophs as revealed by the crystallographic structure in case of bacteria Rhodospirilium rubrum (Schinder et al 1986). It exists as a multimeric protein in case of the higher vascular plants viz Spinach (Chapman et al 1988) and Tobacco (Chapman MS et al 1987). In the present study amino acid sequence analysis of the RuBisCO large chains have been carried out using bioinformatics protocols.