Posttranslation Modification of Plant Protein by Using Bioinformatics
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Dehydrins are highly hydrophilic and thermostable proteins. However, the molecular mechanisms through which they can enhance stress tolerance remain unknown. Non-availability of the dehydrin structure, it is important to analyze its sequence to improve our understanding of amino acids involved in dehydrin functions. Multiple sequence analysis has shown that N-terminus of some of the salt sensitive and salt tolerant plant dehydrins contain DFLGG/KK and DRGLFG/D motif instead of DEYGNP which is found in Aviccenia marina dehydrin. Post translational prediction has revealed myristoylation, phospho...
Dehydrins are highly hydrophilic and thermostable proteins. However, the molecular mechanisms through which they can enhance stress tolerance remain unknown. Non-availability of the dehydrin structure, it is important to analyze its sequence to improve our understanding of amino acids involved in dehydrin functions. Multiple sequence analysis has shown that N-terminus of some of the salt sensitive and salt tolerant plant dehydrins contain DFLGG/KK and DRGLFG/D motif instead of DEYGNP which is found in Aviccenia marina dehydrin. Post translational prediction has revealed myristoylation, phosphorylation and amidation sites. The present study outlines structural and functional aspects of dehydrin which may further assist in understanding their roles in salt stress. Non-specific lipid transfer proteins are small and basic proteins in plants. However, the exact molecular mechanism, through which they can up regulate the expression of lipid transfer proteins which is induced by environmental stresses is still unclear. In present study, we have shown the potential sites of post translational modification in stress tolerant plant mangrove specie Avicennia marina lipid transfer protein.
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