Abstract
S-nitrosylation is a widespread modification of proteins. In plants, most information available to date regarding this modification was obtained using nitric oxide donors and concerned the proteins but not the identification of cysteine residues specifically modified in the proteins or their quantification. Here, we describe a method for the identification of endogenously nitrosylated cysteines in Arabidopsis and, simultaneously, the measurement of relative change in their abundance within binary comparisons.
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Abbreviations
- CID:
-
Collision-induced dissociation
- DMF:
-
Dimethylformamide
- EDTA:
-
Ethylenediaminetetraacetic acid
- ESI-MS/MS:
-
Electrospray ionization-tandem mass spectrometry
- FDR:
-
False discovery rate
- HPLC:
-
High-performance liquid chromatography
- ICAT:
-
Isotope-coded-affinity tag
- MMTS:
-
Methyl methanethiosulfonate
- Q-TOF:
-
Quadrupole-time of flight
- SDS:
-
Sodium dodecyl sulfate
- Th:
-
Thomson is a unit of mass-to-charge ratio
References
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Acknowledgments
A.F. benefited from a PhD grant of the Région Languedoc-Roussillon. The authors acknowledge the help of the INRA Mass Spectrometry Proteomics Platform from the Pole Protéome de Montpellier in performing the analysis.
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Fares, A., Nespoulous, C., Rossignol, M., Peltier, JB. (2014). Simultaneous Identification and Quantification of Nitrosylation Sites by Combination of Biotin Switch and ICAT Labeling. In: Jorrin-Novo, J., Komatsu, S., Weckwerth, W., Wienkoop, S. (eds) Plant Proteomics. Methods in Molecular Biology, vol 1072. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-631-3_41
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DOI: https://doi.org/10.1007/978-1-62703-631-3_41
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Publisher Name: Humana Press, Totowa, NJ
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Online ISBN: 978-1-62703-631-3
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