14-3-3 protein; Phylogenetic and protein interaction, An Insilico analysis
Abstract
14-3-3 proteins are a family of conserved regulatory molecules that have the ability to bind a multitude of functionally diverse signaling proteins, including kinases, phosphatases, and transmembrane receptors.14-3-3 proteins are conserved among many eukaryotic organisms and interact with other target proteins to trigger the transcriptional regulation of genes that generate specific modifications. 14-3-3 proteins are important components in signal transduction pathways affecting multiple plant functions by mediating protein-protein interactions through post-translational modification via phosphorylation .This protein family is involved in a wide range of cellular functions including the regulation of hormonal induction in response to stress stimuli, mediation of symbiotic relationships between the plant host and symbionts, as well as the mediation of functions between cellular components and enzymes. 14-3-3 proteins are an important component in biological pathways involved in the mitigation of biotic and abiotic stresses. This study has been undertaken to study the phylogenetic relationship of the 14-3-3 protein in different plants like Vitis vinifera (Grape), Solanum tuberosum (Potato), Populus tricocarpa (Poplar) and Glycine max (Soyabean). It was observed that 14-3-3 protein is highly conserved across all the different plant species and that the 14-3-3 protein of Solanum tuberosum is closest to Vitis vinifera. The minimum evolutionary distance was observed for Glycine that shows that the14-3-3 protein sequence of Glycine has least diverged from its ancestor. We also studied the protein-protein interactions of the 14-3-3 protein from Solanum tuberosum. The protein is interacting with protein kinases, ATP binding proteins and elongation factors as shown in literature. These interactions are probably helping the protein play a role in combating stress.
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