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Mining for protein S-sulfenylation in Arabidopsis uncovers redox-sensitive sites

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Abstract
Hydrogen peroxide (H2O2) is an important messenger molecule for diverse cellular processes. H2O2 oxidizes proteinaceous cysteinyl thiols to sulfenic acid, also known as S-sulfenylation, thereby affecting the protein conformation and functionality. Although many proteins have been identified as S-sulfenylation targets in plants, site-specific mapping and quantification remain largely unexplored. By means of a peptide-centric chemoproteomics approach, we mapped 1,537 S-sulfenylated sites on more than 1,000 proteins in Arabidopsis thaliana cells. Proteins involved in RNA homeostasis and metabolism were identified as hotspots for S-sulfenylation. Moreover, S-sulfenylation frequently occurred on cysteines located at catalytic sites of enzymes or on cysteines involved in metal binding, hinting at a direct mode of action for redox regulation. Comparison of human and Arabidopsis S-sulfenylation datasets provided 155 conserved S-sulfenylated cysteines, including Cys181 of the Arabidopsis MITOGEN-ACTIVATED PROTEIN KINASE4 (AtMAPK4) that corresponds to Cys161 in the human MAPK1, which has been identified previously as being S-sulfenylated. We show that, by replacing Cys181 of recombinant AtMAPK4 by a redox-insensitive serine residue, the kinase activity decreased, indicating the importance of this noncatalytic cysteine for the kinase mechanism. Altogether, we quantitatively mapped the S-sulfenylated cysteines in Arabidopsis cells under H2O2 stress and thereby generated a comprehensive view on the S-sulfenylation landscape that will facilitate downstream plant redox studies.
Keywords
S-sulfenylation, redox regulation, posttranslational modification, Arabidopsis, chemoproteomics, OXIDATIVE STRESS, CYSTEINE SULFENYLATION, HYDROGEN-PEROXIDE, TARGET PROTEIN, MAP KINASES, NITROSYLATION, THALIANA, IDENTIFICATION, DEHYDROGENASE, GLUTAREDOXINS

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MLA
Huang, Jingjing, et al. “Mining for Protein S-Sulfenylation in Arabidopsis Uncovers Redox-Sensitive Sites.” PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, vol. 116, no. 42, 2019, pp. 21256–61.
APA
Huang, J., Willems, P., Wei, B., Tian, C., Ferreira, R. B., Bodra, N., … Messens, J. (2019). Mining for protein S-sulfenylation in Arabidopsis uncovers redox-sensitive sites. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 116(42), 21256–21261.
Chicago author-date
Huang, Jingjing, Patrick Willems, Bo Wei, Caiping Tian, Renan B Ferreira, Nandita Bodra, Santiago Agustín Martínez Gache, et al. 2019. “Mining for Protein S-Sulfenylation in Arabidopsis Uncovers Redox-Sensitive Sites.” PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 116 (42): 21256–61.
Chicago author-date (all authors)
Huang, Jingjing, Patrick Willems, Bo Wei, Caiping Tian, Renan B Ferreira, Nandita Bodra, Santiago Agustín Martínez Gache, Khadija Wahni, Keke Liu, Didier Vertommen, Kris Gevaert, Kate S Carroll, Marc Van Montagu, Jing Yang, Frank Van Breusegem, and Joris Messens. 2019. “Mining for Protein S-Sulfenylation in Arabidopsis Uncovers Redox-Sensitive Sites.” PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 116 (42): 21256–21261.
Vancouver
1.
Huang J, Willems P, Wei B, Tian C, Ferreira RB, Bodra N, et al. Mining for protein S-sulfenylation in Arabidopsis uncovers redox-sensitive sites. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 2019;116(42):21256–61.
IEEE
[1]
J. Huang et al., “Mining for protein S-sulfenylation in Arabidopsis uncovers redox-sensitive sites,” PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, vol. 116, no. 42, pp. 21256–21261, 2019.
@article{8631988,
  abstract     = {Hydrogen peroxide (H2O2) is an important messenger molecule for diverse cellular processes. H2O2 oxidizes proteinaceous cysteinyl thiols to sulfenic acid, also known as S-sulfenylation, thereby affecting the protein conformation and functionality. Although many proteins have been identified as S-sulfenylation targets in plants, site-specific mapping and quantification remain largely unexplored. By means of a peptide-centric chemoproteomics approach, we mapped 1,537 S-sulfenylated sites on more than 1,000 proteins in Arabidopsis thaliana cells. Proteins involved in RNA homeostasis and metabolism were identified as hotspots for S-sulfenylation. Moreover, S-sulfenylation frequently occurred on cysteines located at catalytic sites of enzymes or on cysteines involved in metal binding, hinting at a direct mode of action for redox regulation. Comparison of human and Arabidopsis S-sulfenylation datasets provided 155 conserved S-sulfenylated cysteines, including Cys181 of the Arabidopsis MITOGEN-ACTIVATED PROTEIN KINASE4 (AtMAPK4) that corresponds to Cys161 in the human MAPK1, which has been identified previously as being S-sulfenylated. We show that, by replacing Cys181 of recombinant AtMAPK4 by a redox-insensitive serine residue, the kinase activity decreased, indicating the importance of this noncatalytic cysteine for the kinase mechanism. Altogether, we quantitatively mapped the S-sulfenylated cysteines in Arabidopsis cells under H2O2 stress and thereby generated a comprehensive view on the S-sulfenylation landscape that will facilitate downstream plant redox studies.},
  author       = {Huang, Jingjing and Willems, Patrick and Wei, Bo and Tian, Caiping and Ferreira, Renan B and Bodra, Nandita and Martínez Gache, Santiago Agustín and Wahni, Khadija and Liu, Keke and Vertommen, Didier and Gevaert, Kris and Carroll, Kate S and Van Montagu, Marc and Yang, Jing and Van Breusegem, Frank and Messens, Joris},
  issn         = {0027-8424},
  journal      = {PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA},
  keywords     = {S-sulfenylation,redox regulation,posttranslational modification,Arabidopsis,chemoproteomics,OXIDATIVE STRESS,CYSTEINE SULFENYLATION,HYDROGEN-PEROXIDE,TARGET PROTEIN,MAP KINASES,NITROSYLATION,THALIANA,IDENTIFICATION,DEHYDROGENASE,GLUTAREDOXINS},
  language     = {eng},
  number       = {42},
  pages        = {21256--21261},
  title        = {Mining for protein S-sulfenylation in Arabidopsis uncovers redox-sensitive sites},
  url          = {http://dx.doi.org/10.1073/pnas.1906768116},
  volume       = {116},
  year         = {2019},
}

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