ABSTRACT: Analysis of flg22-induced transcriptional changes in mpk3, mpk4 and mpk6 mutants. - 2 weeks old seedlings compared for transcriptome after a 30min mock or 1µM flg22 treatment.
Project description:inra12-05_mut_flg_ii-FLG-MPKs ra12-05_mut_flg_ii - inra12-05_mut_flg_ii - Analysis of flg22-induced transcriptional changes in mpk3, mpk4 and mpk6 mutants. - 2 weeks old seedlings compared for transcriptome after a 30min mock or 1µM flg22 treatment.
Project description:inra12-05_mut_flg_ii-FLG-MPKs ra12-05_mut_flg_ii - inra12-05_mut_flg_ii - Analysis of flg22-induced transcriptional changes in mpk3, mpk4 and mpk6 mutants. - 2 weeks old seedlings compared for transcriptome after a 30min mock or 1µM flg22 treatment. 21 dye-swap - gene knock out,normal vs mutant comparison,treated vs untreated comparison
Project description:ra12-01_mut_flg - inra12-01_mut-flg - Analysis of flg22-induced transcriptional changes in oxi1, OXI1oe, pti1-4, CA-MPK4 and ice1 mutant lines - 2 weeks seedlings compared for their transcriptome after a 30min mock or 1µM flg22 treatment.
Project description:Arabidopsis MPK11 is activated and plays a role in the flg22 sensing. Mitogen-activated protein kinases (MAPKs) mediate cellular signal transduction during stress responses, as well as diverse growth and developmental steps in eukaryotes. Pathogen infection or treatment with conserved pathogen-associated molecular patterns (PAMPs) such as the bacterial flagellin-derived flg22 peptide are known to activate three Arabidopsis thaliana MAPKs, MPK3, MPK4 and MPK6. Several stresses, including flg22 treatment, are known to increase MPK11 expression but activation of MPK11 has not been shown. Here, we show that MPK11 activity can indeed be increased through flg22 elicitation. Expression profiling using a small-scale microarray for defense-related genes revealed that cinnamyl alcohol dehyrogenase 5 (CAD5) requires MPK11 for full flg22-induced expression. An mpk11 mutant showed increased flg22-mediated growth inhibition but no altered susceptibility to Pseudomonas syringae, Botrytis cinerea or Alternaria brassicicola.
Project description:Arabidopsis MPK11 is activated and plays a role in the flg22 sensing. Mitogen-activated protein kinases (MAPKs) mediate cellular signal transduction during stress responses, as well as diverse growth and developmental steps in eukaryotes. Pathogen infection or treatment with conserved pathogen-associated molecular patterns (PAMPs) such as the bacterial flagellin-derived flg22 peptide are known to activate three Arabidopsis thaliana MAPKs, MPK3, MPK4 and MPK6. Several stresses, including flg22 treatment, are known to increase MPK11 expression but activation of MPK11 has not been shown. Here, we show that MPK11 activity can indeed be increased through flg22 elicitation. Expression profiling using a small-scale microarray for defense-related genes revealed that cinnamyl alcohol dehyrogenase 5 (CAD5) requires MPK11 for full flg22-induced expression. An mpk11 mutant showed increased flg22-mediated growth inhibition but no altered susceptibility to Pseudomonas syringae, Botrytis cinerea or Alternaria brassicicola. A 24 DNA microarray study using toral RNA from an Arabidopsis mutant (mpk11 SALK049352) as well as wild type treated with water or flg22.
Project description:In Arabidopsis, mitogen-activated protein kinases MPK3, MPK4 and MPK6 constitute essential relays for a variety of functions including cell division, development and innate immunity. While some substrates of MPK3, MPK4 and MPK6 have been identified, the picture is still far from complete. To identify substrates of these MAPKs in cell division, growth and development we compared the phosphoproteomes of wild-type and mpk3, mpk4 and mpk6. To study the function of these MAPKs in innate immunity, we analyzed their phosphoproteomes following activation by a microbe-associated molecular pattern (MAMP). Partially overlapping substrates were retrieved for all three MAPKs, showing target specificity to one, two or all three MAPKs in different biological processes. More precisely, our results illustrate the fact that the entity to be defined as a specific or a shared substrate for MAPKs is not a phosphoprotein but a particular (S/T)P phosphorylation site in a given protein. As a whole, 152 peptides were identified to be differentially phosphorylated in response to MAMP treatment and/or when compared between genotypes and 70 of them could be classified as putative MAPK targets. Biochemical analysis of a number of putative MAPK substrates by phosphorylation and interaction assays confirmed the global phosphoproteome approach. Our study finally expands the set of MAPK substrates to involve other protein kinases, including calcium-dependent (CDPK) and sugar non-fermenting (SnRK) protein kinases.
