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dc.contributor.advisorRajasekhran, Ram
dc.contributor.authorIyappan, R
dc.date.accessioned2018-07-19T07:06:51Z
dc.date.accessioned2018-07-30T14:14:06Z
dc.date.available2018-07-19T07:06:51Z
dc.date.available2018-07-30T14:14:06Z
dc.date.issued2018-07-19
dc.date.submitted2015
dc.identifier.urihttp://etd.iisc.ac.in/handle/2005/3861
dc.identifier.abstracthttp://etd.iisc.ac.in/static/etd/abstracts/4733/G26896-Abs.pdfen_US
dc.description.abstractProtein phosphorylation is a key cellular regulatory mechanism. Phosphorylation can either activate or inhibit the function of a particular protein. Activation of protein kinases has been implicated in response to light, pathogen attack, growth regulators, stress and nutrient deficiency in plants. Most of the intracellular signaling pathways use protein phosphorylation to create signals and conduct them further. Identification of the physiological substrates for the protein kinase enables the understanding of how the signaling networks function and how they are disturbed under adverse conditions. Identification of the physiological substrates for the kinase is limited by the low stoichiometry of protein phosphorylation inside the cell. Although, recent advances in mass spectrometric techniques have increased the identification of phosphorylated protein in the cell, the precise connection between the kinase and identified phosphorylated protein is not established. Dual-specificity kinases that phosphorylate on serine, threonine and tyrosine residues have been identified and characterized in plants. However, the in vivo substrates for most of these kinases have not been identified. Recently a manganese-dependent dual-specificity STY protein kinase (STYK) has been identified from Arabidopsis thaliana which has been suggested to play a role in plant growth, development and in systemic acquired resistance. The identification of the physiological substrate for AtSTYK may help in understanding the signal transduction pathway the kinase in involved and how it is perturbed in different physiological condition. Therefore, the main objectives of my current study are,  To identify the physiological substrates of the AtSTY dual specificity kinase (STYK). 1) Identification of the substrates by using genetic, proteomic and biochemical approaches. 2) Biochemical characterization of the substrate phosphorylation. 3) Identifying the biochemical function of the substrate protein. 4) Assessing the significance of substrate phosphorylation.en_US
dc.language.isoen_USen_US
dc.relation.ispartofseriesG26896en_US
dc.subjectLipid Metabolismen_US
dc.subjectProtein Kinaseen_US
dc.subjectArbidopsis Thaliana Proteinsen_US
dc.subjectPlant Protein Kinasesen_US
dc.subjectArabidopsis Dual Specificity STY Protein Kinase (AtSTYK)en_US
dc.subjectArabidopsis Serine/Theronine Kinasesen_US
dc.subjectArabidopsis Tyrosine Kinasesen_US
dc.subjectPlants Growthen_US
dc.subjectSTY Protein Kinaseen_US
dc.subjectArabidopsis thalianaen_US
dc.subjectOleosin 1en_US
dc.subjectSerine/threonine/tyrosine Protein Kinaseen_US
dc.subjectLysophosphatidic Acid Phosphataseen_US
dc.subject.classificationPlant Physiologyen_US
dc.titleArabidopsis Serine/Threonine/Tyrosine Protein Kinase : Implications in Growth And DEvelopmenten_US
dc.typeThesisen_US
dc.degree.namePhDen_US
dc.degree.levelDoctoralen_US
dc.degree.disciplineFaculty of Scienceen_US


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