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RESEARCH PRODUCT
Activation of MAPK homologues by elicitors in tobacco cells
Fatma OuakedAnnick ChiltzAlain PuginAngela Lebrun-garciasubject
0106 biological sciencesCalcium-Calmodulin-Dependent Protein Kinases0303 health sciencesbiologyKinaseNicotiana tabacumPhosphataseCell BiologyPlant Sciencebiology.organism_classification01 natural sciences3. Good health03 medical and health sciencesBiochemistryMitogen-activated protein kinaseGeneticsbiology.proteinmedicinePhosphorylationStaurosporineProtein kinase A030304 developmental biology010606 plant biology & botanymedicine.drugdescription
Elicitors of plant defence reactions (such as cryptogein, an elicitin produced by Phytophthora cryptogea, or oligogalacturonides (OGs)), induced in tobacco cell suspensions (Nicotiana tabacum var Xanthi) a rapid and transient activation of two protein kinases (PKs) with apparent molecular masses of 50 and 46 kDa, respectively. These PKs activated and phosphorylated at tyrosine residues, phosphorylated myelin basic protein (MBP) at serine/threonine residues. Both are recognized by anti-MAPK antibodies. The two MBP kinases possessed the same kinetics of activation, and their activation depended, to the same extent, on different exogenously applied compounds (staurosporine, lanthanum, EGTA). We demonstrate here that the activation of the MBP kinases is calcium dependent and sensitive to staurosporine, a protein kinase inhibitor which annihilates all known responses of tobacco cells to cryptogein. The activation of MBP kinases appeared to be independent of the production of active oxygen species (AOS) and insensitive to calyculin A, a protein phosphatase type 1 and 2A inhibitor. The activation of MAPKs is discussed in relation to the early responses induced by cryptogein.
year | journal | country | edition | language |
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1998-09-01 | The Plant Journal |