Mass Spectrometric-Based Selected Reaction Monitoring of Protein Phosphorylation during Symbiotic Signaling in the Model Legume, Medicago truncatula
Autor: | Michael R. Sussman, Dhileepkumar Jayaraman, Jean-Michel Ané, Gregory A. Barrett-Wilt, Lori K. Van Ness, Junko Maeda |
---|---|
Rok vydání: | 2016 |
Předmět: |
0106 biological sciences
0301 basic medicine Cell Membranes lcsh:Medicine Biochemistry 01 natural sciences Mass Spectrometry Serine Cell Signaling Gene Expression Regulation Plant Protein phosphorylation Phosphorylation Post-Translational Modification Threonine lcsh:Science Plant Proteins 2. Zero hunger Multidisciplinary Protein Kinase Signaling Cascade Kinase food and beverages Plants Legumes Signaling Cascades Medicago truncatula Engineering and Technology Cellular Structures and Organelles Signal transduction Rhizobium Signal Transduction Research Article Biology 03 medical and health sciences Symbiosis lcsh:R Organisms Biology and Life Sciences Proteins Membrane Proteins Cell Biology biology.organism_classification Species Interactions 030104 developmental biology Seedlings Signal Processing lcsh:Q 010606 plant biology & botany |
Zdroj: | PLoS ONE, Vol 11, Iss 5, p e0155460 (2016) PLoS ONE |
ISSN: | 1932-6203 |
Popis: | Unlike the major cereal crops corn, rice, and wheat, leguminous plants such as soybean and alfalfa can meet their nitrogen requirement via endosymbiotic associations with soil bacteria. The establishment of this symbiosis is a complex process playing out over several weeks and is facilitated by the exchange of chemical signals between these partners from different kingdoms. Several plant components that are involved in this signaling pathway have been identified, but there is still a great deal of uncertainty regarding the early events in symbiotic signaling, i.e., within the first minutes and hours after the rhizobial signals (Nod factors) are perceived at the plant plasma membrane. The presence of several protein kinases in this pathway suggests a mechanism of signal transduction via posttranslational modification of proteins in which phosphate is added to the hydroxyl groups of serine, threonine and tyrosine amino acid side chains. To monitor the phosphorylation dynamics and complement our previous untargeted 'discovery' approach, we report here the results of experiments using a targeted mass spectrometric technique, Selected Reaction Monitoring (SRM) that enables the quantification of phosphorylation targets with great sensitivity and precision. Using this approach, we confirm a rapid change in the level of phosphorylation in 4 phosphosites of at least 4 plant phosphoproteins that have not been previously characterized. This detailed analysis reveals aspects of the symbiotic signaling mechanism in legumes that, in the long term, will inform efforts to engineer this nitrogen-fixing symbiosis in important non-legume crops such as rice, wheat and corn. |
Databáze: | OpenAIRE |
Externí odkaz: |