RuBisCO is the main photosynthetic enzyme of carbon assimilatory pathways in nature. Despite being the most abundant protein on earth, RuBisCO is still relatively underutilized in the food chain. Although having sequence and structure details in the database, studies on evolutionary relationships have few instances. A bioinformatics and in silico study was conducted to check sequence and structural differences of RuBisCO among different photosynthetic organisms. RuBisCO from Oryza sativa showed abundance of charged amino acids, salt-bridges and intra-protein interactions and was more hydrophilic in nature compared to Nostoc sp., Chlamydomonas reinhardtii, and Nicotiana tabacum. From molecular dynamics simulations, lower root mean square deviation and root mean square fluctuation indicate that RuBisCO from Oryza sativa was more stable followed by Nicotiana tabacum and lower radius of gyrations indicates their tightly packing. From this study, it was clear that some specific evolutions in charged amino acids of RuBisCO of monocot i.e., Oryza sativa make it more stable and stronger than other plant groups. The study concludes more stable nature of RuBisCO from monocot Oryza sativa.
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Comparative analysis of RuBisCO evolution and intrinsic differences: insights from in silico assessment in cyanobacteria, monocot and dicot plants
Published: 08 January 2024 by MDPI in The 3rd International Electronic Conference on Agronomy session Plant breeding, genetics, genomics and biotechnology
Keywords: RuBisCO, Evolution, Salt-Bridge, Intra-protein interactions, Molecular Dynamic Simulations.