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In vivo detection of protein cysteine sulfenylation in plastids

(2019) PLANT JOURNAL. 97(4). p.765-778
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Abstract
Protein cysteine thiols are post‐translationally modified under oxidative stress conditions. Illuminated chloroplasts are one of the important sources of hydrogen peroxide (H2O2) and are highly sensitive to environmental stimuli, yet a comprehensive view of the oxidation‐sensitive chloroplast proteome is still missing. By targeting the sulfenic acid YAP1C‐trapping technology to the plastids of light‐grown Arabidopsis cells, we identified 132 putatively sulfenylated plastid proteins upon H2O2 pulse treatment. Almost half of the sulfenylated proteins are enzymes of the amino acid metabolism. Using metabolomics, we observed a reversible decrease in the levels of the amino acids Ala, Asn, Cys, Gln, Glu, His, Ile, Leu, Lys, Phe, Ser, Thr and Val after H2O2 treatment, which is in line with an anticipated decrease in the levels of the glycolysis and tricarboxylic acid metabolites. Through the identification of an organelle‐tailored proteome, we demonstrated that the subcellular targeting of the YAP1C probe enables us to study in vivo cysteine sulfenylation at the organellar level. All in all, the identification of these oxidation events in plastids revealed that several enzymes of the amino acid metabolism rapidly undergo cysteine oxidation upon oxidative stress.
Keywords
sulfenic acid, plastid, amino acid metabolism, PTM, oxidative stress, redox signaling, Arabidopsis thaliana, THIOREDOXIN TARGET PROTEINS, REDOX-SENSITIVE PROTEINS, OXIDATIVE STRESS, MASS-SPECTROMETRY, COMPREHENSIVE SURVEY, METABOLIC-RESPONSE, CHLOROPLAST STROMA, ARABIDOPSIS, IDENTIFICATION, PROTEOMICS

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Citation

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MLA
De Smet, Barbara et al. “In Vivo Detection of Protein Cysteine Sulfenylation in Plastids.” PLANT JOURNAL 97.4 (2019): 765–778. Print.
APA
De Smet, Barbara, Willems, P., Fernández Fernández, A. D., Alseekh, S., Fernie, A. R., Messens, J., & Van Breusegem, F. (2019). In vivo detection of protein cysteine sulfenylation in plastids. PLANT JOURNAL, 97(4), 765–778.
Chicago author-date
De Smet, Barbara, Patrick Willems, Alvaro Daniel Fernández Fernández, Saleh Alseekh, Alisdair R Fernie, Joris Messens, and Frank Van Breusegem. 2019. “In Vivo Detection of Protein Cysteine Sulfenylation in Plastids.” Plant Journal 97 (4): 765–778.
Chicago author-date (all authors)
De Smet, Barbara, Patrick Willems, Alvaro Daniel Fernández Fernández, Saleh Alseekh, Alisdair R Fernie, Joris Messens, and Frank Van Breusegem. 2019. “In Vivo Detection of Protein Cysteine Sulfenylation in Plastids.” Plant Journal 97 (4): 765–778.
Vancouver
1.
De Smet B, Willems P, Fernández Fernández AD, Alseekh S, Fernie AR, Messens J, et al. In vivo detection of protein cysteine sulfenylation in plastids. PLANT JOURNAL. 2019;97(4):765–78.
IEEE
[1]
B. De Smet et al., “In vivo detection of protein cysteine sulfenylation in plastids,” PLANT JOURNAL, vol. 97, no. 4, pp. 765–778, 2019.
@article{8599143,
  abstract     = {Protein cysteine thiols are post‐translationally modified under oxidative stress conditions. Illuminated chloroplasts are one of the important sources of hydrogen peroxide (H2O2) and are highly sensitive to environmental stimuli, yet a comprehensive view of the oxidation‐sensitive chloroplast proteome is still missing. By targeting the sulfenic acid YAP1C‐trapping technology to the plastids of light‐grown Arabidopsis cells, we identified 132 putatively sulfenylated plastid proteins upon H2O2 pulse treatment. Almost half of the sulfenylated proteins are enzymes of the amino acid metabolism. Using metabolomics, we observed a reversible decrease in the levels of the amino acids Ala, Asn, Cys, Gln, Glu, His, Ile, Leu, Lys, Phe, Ser, Thr and Val after H2O2 treatment, which is in line with an anticipated decrease in the levels of the glycolysis and tricarboxylic acid metabolites. Through the identification of an organelle‐tailored proteome, we demonstrated that the subcellular targeting of the YAP1C probe enables us to study in vivo cysteine sulfenylation at the organellar level. All in all, the identification of these oxidation events in plastids revealed that several enzymes of the amino acid metabolism rapidly undergo cysteine oxidation upon oxidative stress.},
  author       = {De Smet, Barbara and Willems, Patrick and Fernández Fernández, Alvaro Daniel and Alseekh, Saleh and Fernie, Alisdair R and Messens, Joris and Van Breusegem, Frank},
  issn         = {0960-7412},
  journal      = {PLANT JOURNAL},
  keywords     = {sulfenic acid,plastid,amino acid metabolism,PTM,oxidative stress,redox signaling,Arabidopsis thaliana,THIOREDOXIN TARGET PROTEINS,REDOX-SENSITIVE PROTEINS,OXIDATIVE STRESS,MASS-SPECTROMETRY,COMPREHENSIVE SURVEY,METABOLIC-RESPONSE,CHLOROPLAST STROMA,ARABIDOPSIS,IDENTIFICATION,PROTEOMICS},
  language     = {eng},
  number       = {4},
  pages        = {765--778},
  title        = {In vivo detection of protein cysteine sulfenylation in plastids},
  url          = {http://dx.doi.org/10.1111/tpj.14146},
  volume       = {97},
  year         = {2019},
}

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