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KMID : 0368420170600010035
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Journal of Plant Biology
2017 Volume.60 No. 1 p.35 ~ p.47
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Computational study of biochemical properties of ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) enzyme in C3 plants
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Darabi Maryam
Seddigh Samin
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Abstract
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Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO; EC 4.1.1.39) is a key enzyme in plant photosynthesis that catalyzes the reaction in the photosynthetic assimilation of atmospheric carbon dioxide (CO2). In this study, bioinformatic characterization of RuBisCO enzyme was performed in protein sequences of its large subunits (rbcL) from 25 C3 plants of 14 different families. In protein-protein interactions analysis by STRING 10 tool, 7 and 168 relevant datasets were identified in Arabidopsis thaliana and other species, respectively. The structural and functional analyses were investigated by ProtParam, SOPMA, Predotar 1.03, SignalP 4.1, TargetP 1.1, and TMHMM 2.0 tools in ExPASy database. Tertiary structure was predicted by Phyre2 and TM-score servers then their qualities were verified by PROCHECK and SuperPose servers. In MEME and MAST analyses, 9 common conserved motifs obtained in all C3 plants. The protein sequences were aligned with ClustalW algorithm by MEGA 6.06 software and phylogenetic tree was constructed using the Neighbor-joining (NJ) method. According to the results, there is a high identity of RuBisCO in different species of C3 plants so that they should be derived from a common ancestor. The results provide background of bioinformatic studies for the function and evolution of RuBisCO in other plants.
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KEYWORD
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Bioinformatics, Phylogenetic analysis, Proteinprotein interaction, Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase (RuBisCO), Structural analysis
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