Abstract
Nitric oxide is regarded as a key signaling messenger in several organisms. Its physiological relevance is partly due to its capacity to induce posttranslational modifications of proteins through its direct or indirect reaction with specific amino acid residues. Among them, S-nitrosylation has been shown to be involved in a broad range of cellular signaling pathways both in animals and plants. The identification of S-nitrosylated proteins has been made possible by the development of the Biotin-Switch Technique (BST) in the early 2000s. Here, we describe the BST protocol we routinely use to check in vitro S-nitrosylation of recombinant proteins induced by NO donors.
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References
Hill AC, Bennett JH (1970) Inhibition of apparent photosynthesis by nitrogen oxides. Atmospheric Environ (1967) 4:341–348
Noritake T, Kawakita K, Doke N (1996) Nitric oxide induces phytoalexin accumulation in potato tuber tissues. Plant Cell Physiol 37:113–116
Delledonne M, Xia Y, Dixon RA et al (1998) Nitric oxide functions as a signal in plant disease resistance. Nature 394:585–588
Durner J, Wendehenne D, Klessig DF (1998) Defense gene induction in tobacco by nitric oxide, cyclic GMP, and cyclic ADP-ribose. Proc Natl Acad Sci U S A 95:10328–10333
Yu M, Lamattina L, Spoel S et al (2014) Nitric oxide function in plant biology: a redox cue in deconvolution. New Phytol 202:1142–1156
Zaffagnini M, De Mia M, Morisse S et al (2016) Protein S-nitrosylation in photosynthetic organisms: a comprehensive overview with future perspectives. Biochim Biophys Acta 1864:952–966
Lamotte O, Bertoldo JB, Besson-Bard A et al (2015) Protein S-nitrosylation: specificity and identification strategies in plants. Front Chem 2:114. https://doi.org/10.3389/fchem.2014.00114
Jaffrey SR, Erdjument-Bromage H, Ferris CD et al (2001) Protein S-nitrosylation: a physiological signal for neuronal nitric oxide. Nat Cell Biol 3:193–19
Lindermayr C, Saalbach G, Durner J (2005) Proteomic identification of S-nitrosylated proteins in arabidopsis. Plant Physiol 137:921–930
Abat JK, Mattoo AK, Deswal R (2008) S-nitrosylated proteins of a medicinal CAM plant Kalanchoe pinnata – ribulose-1,5-bisphosphate carboxylase/oxygenase activity targeted for inhibition. FEBS J 275:2862–2872
Romero-Puertas MC, Campostrini N, Mattè A et al (2008) Proteomic analysis of S-nitrosylated proteins in Arabidopsis thaliana undergoing hypersensitive response. Proteomics 8:1459–1469
Abat JK, Deswal R (2009) Differential modulation of S-nitrosoproteome of Brassica juncea by low temperature: change in S-nitrosylation of Rubisco is responsible for the inactivation of its carboxylase activity. Proteomics 9:4368–4380
Palmieri MC, Lindermayr C, Bauwe H et al (2010) Regulation of plant glycine decarboxylase by S-nitrosylation and glutathionylation. Plant Physiol 152:1514–1528
Ortega-Galisteo AP, Rodriguez-Serrano M, Pazmino DM et al (2012) S-Nitrosylated proteins in pea (Pisum sativum L.) leaf peroxisomes: changes under abiotic stress. J Exp Bot 63:2089–2103
Kato H, Takemoto D, Kawakita K (2013) Proteomic analysis of S-nitrosylated proteins in potato plant. Physiol Plant 148:371–386
Maldonado-Alconada AM, Echevarria-Zomeno S, Lindermayr C et al (2011) Proteomic analysis of Arabidopsis protein S-nitrosylation in response to inoculation with Pseudomonas syringae. Acta Physiol Plant 33:1493–1514
Astier J, Besson-Bard A, Lamotte O et al (2012) Nitric oxide inhibits the ATPase activity of the chaperone-like AAA+ ATPase CDC48, a target for S-nitrosylation in cryptogein signalling in tobacco cells. Biochem J 447:249–260
Puyaubert J, Fares A, Rézé N et al (2014) Identification of endogenously S-nitrosylated proteins in Arabidopsis plantlets: effect of cold stress on cysteine nitrosylation level. Plant Sci 215-216:150–156
Vanzo E, Ghirardo A, Merl-Pham J et al (2014) S-nitroso-proteome in poplar leaves in response to acute ozone stress. PLoS One 9(9):e106886. https://doi.org/10.1371/journal.pone.0106886
Fares A, Rossignol M, Peltier JB (2011) Proteomics investigation of endogenous S-nitrosylation in Arabidopsis. Biochem Biophys Res Commun 416:331–336
Rosnoblet C, Bègue H, Blanchard C et al (2017) Functional characterization of the chaperon-like protein Cdc48 in cryptogein-induced immune response in tobacco. Plant Cell Environ 40:491–508
Seth D, Stamler JS (2011) The SNO-proteome: causation and classifications. Curr Opin Chem Biol 15:129–136
Wang Y-Q, Feechan A, Yun B-W et al (2009) S-nitrosylation of AtSABP3 antagonizes the expression of plant immunity. J Biol Chem 284(4):2131–2137
Maeda H, Dudareva N (2012) The shikimate pathway and aromatic amino acid biosynthesis in plants. Ann Rev Plant Biol 63:73–105
Zhelyaskov VR, Gee KR, Godwin DW (1998) Control of NO concentration in solutions of nitrosothiol compounds by light. Photochem Photobiol 67:282–288
Forrester MT, Foster MW, Stamler JS (2007) Assessment and application of the biotin switch technique for examining protein S-nitrosylation under conditions of pharmacologically induced oxidative stress. J Biol Chem 11:13977–13983
Veleeparampil MM, Aravind UK, Aravindakumar CT (2009) Decomposition of S-nitrosothiols induced by UV and sunlight. Adv Phys Chem 2009:1–5
Gallagher SR (2012) One-dimensional SDS gel electrophoresis of proteins. Curr Protoc Protein Sci 68(10.1):10.1.1–10.1.44
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Aimé, S., Hichami, S., Wendehenne, D., Lamotte, O. (2018). Analysis of Recombinant Protein S-Nitrosylation Using the Biotin-Switch Technique. In: Mengel, A., Lindermayr, C. (eds) Nitric Oxide. Methods in Molecular Biology, vol 1747. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-7695-9_11
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DOI: https://doi.org/10.1007/978-1-4939-7695-9_11
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