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Sulfenylated proteins in the Medicago truncatula-Sinorhizobium meliloti symbiosis
- Source :
- Journal of Proteomics, Journal of Proteomics, Elsevier, 2012, 75 (13), pp.4102-4113. ⟨10.1016/j.jprot.2012.05.024⟩
- Publication Year :
- 2012
- Publisher :
- HAL CCSD, 2012.
-
Abstract
- International audience; Reactive oxygen species such as hydrogen peroxide (H2O2), play a crucial role as signaling molecules in the establishment and functioning of the nitrogen-fixing legume-Rhizobium symbiosis. The regulation of protein function through oxidative modification has emerged as an important molecular mechanism modulating various biological processes. Protein cysteine residues are known to be sensitive targets of H2O2, in a posttranslational modification called sulfenylation. We trapped and identified sulfenylated proteins in the Medicago truncatula-Sinorhizobium meliloti symbiosis, by combining the use of chemical and genetic probes with mass spectrometry analysis. We identified 44 M. truncatula proteins sulfenylated in inoculated roots (two days post infection, 2 dpi) and 65 such proteins in the functioning symbiotic organ, the nodule (four weeks post infection, 4 wpi); 18 proteins were identified at both time points. However, the largest functional groups at 2 dpi and 4 wpi were different: redox state-linked proteins early in the interaction and proteins involved in amino-acid and carbohydrate metabolism in the nodule. Twenty proteins from S. meliloti, including some directly involved in nitrogen fixation, were also identified as sulfenylated. These results suggest that sulfenylation may regulate the activity of proteins playing major roles in the development and functioning of the symbiotic interaction. (c) 2012 Elsevier B.V. All rights reserved.
- Subjects :
- 0106 biological sciences
Sulfenylation
ENHANCED SUCROSE SYNTHASE
Cell signaling
Root nodule
H2O2
[SDV]Life Sciences [q-bio]
Biophysics
SIGNAL-TRANSDUCTION
Biology
01 natural sciences
Biochemistry
Sulfenic Acids
03 medical and health sciences
HYDROGEN-PEROXIDE
Bacterial Proteins
Symbiosis
GENETICALLY ENCODED PROBE
Nitrogen Fixation
Medicago truncatula
SULFENIC ACFORMATION
GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE
ROOT-NODULES
Plant Proteins
030304 developmental biology
0303 health sciences
Sinorhizobium meliloti
CYSTEINE OXIDATION
food and beverages
Hydrogen Peroxide
biology.organism_classification
Medicago truncatula-Sinorhizobium
[SDE]Environmental Sciences
Rhizobium
meliloti symbiosis
Posttranslational modification
DISULFIDE BOND FORMATION
REACTIVE OXYGEN
Signal transduction
Protein Processing, Post-Translational
010606 plant biology & botany
Cysteine
Subjects
Details
- Language :
- English
- ISSN :
- 18743919 and 18767737
- Database :
- OpenAIRE
- Journal :
- Journal of Proteomics, Journal of Proteomics, Elsevier, 2012, 75 (13), pp.4102-4113. ⟨10.1016/j.jprot.2012.05.024⟩
- Accession number :
- edsair.doi.dedup.....d569c7064ea46e2a02f1715c6801cf57