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Cysteines under ROS attack in plants: a proteomics view

(2015) JOURNAL OF EXPERIMENTAL BOTANY. 66(10). p.2935-2944
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Biotechnology for a sustainable economy (Bio-Economy)
Abstract
Plants generate reactive oxygen species (ROS) as part of their metabolism and in response to various external stress factors, potentially causing significant damage to biomolecules and cell structures. During the course of evolution, plants have adapted to ROS toxicity, and use ROS as signalling messengers that activate defence responses. Cysteine (Cys) residues in proteins are one of the most sensitive targets for ROS-mediated post-translational modifications, and they have become key residues for ROS signalling studies. The reactivity of Cys residues towards ROS, and their ability to react to different oxidation states, allow them to appear at the crossroads of highly dynamic oxidative events. As such, a redox-active cysteine can be present as S-glutathionylated (-SSG), disulfide bonded (S-S), sulfenylated (-SOH), sulfinylated (-SO2H), and sulfonylated (-SO3H). The sulfenic acid (-SOH) form has been considered as part of ROS-sensing pathways, as it leads to further modifications which affect protein structure and function. Redox proteomic studies are required to understand how and why cysteines undergo oxidative post-translational modifications and to identify the ROS-sensor proteins. Here, we update current knowledge of cysteine reactivity with ROS. Further, we give an overview of proteomic techniques that have been applied to identify different redox-modified cysteines in plants. There is a particular focus on the identification of sulfenylated proteins, which have the potential to be involved in plant signal transduction.
Keywords
REDOX REGULATION, NITRIC-OXIDE, HYDROGEN-PEROXIDE, ARABIDOPSIS-THALIANA, ACTIVE-SITE CYSTEINE, S-NITROSYLATED PROTEINS, DISULFIDE BOND FORMATION, redox proteomics, THIOREDOXIN TARGET PROTEINS, SULFENIC ACID FORMATION, sulfenic acid, GENETICALLY ENCODED PROBE, redox regulation, reactive oxygen species (ROS), oxidative post-translational modification, Cysteine (Cys)

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Citation

Please use this url to cite or link to this publication:

MLA
Akter, Mosammat Salma et al. “Cysteines Under ROS Attack in Plants: a Proteomics View.” JOURNAL OF EXPERIMENTAL BOTANY 66.10 (2015): 2935–2944. Print.
APA
Akter, M. S., Huang, J., Waszczak, C., Jacques, S., Gevaert, K., Van Breusegem, F., & Messens, J. (2015). Cysteines under ROS attack in plants: a proteomics view. JOURNAL OF EXPERIMENTAL BOTANY, 66(10), 2935–2944.
Chicago author-date
Akter, Mosammat Salma, Jingjing Huang, Cezary Waszczak, Silke Jacques, Kris Gevaert, Frank Van Breusegem, and Joris Messens. 2015. “Cysteines Under ROS Attack in Plants: a Proteomics View.” Journal of Experimental Botany 66 (10): 2935–2944.
Chicago author-date (all authors)
Akter, Mosammat Salma, Jingjing Huang, Cezary Waszczak, Silke Jacques, Kris Gevaert, Frank Van Breusegem, and Joris Messens. 2015. “Cysteines Under ROS Attack in Plants: a Proteomics View.” Journal of Experimental Botany 66 (10): 2935–2944.
Vancouver
1.
Akter MS, Huang J, Waszczak C, Jacques S, Gevaert K, Van Breusegem F, et al. Cysteines under ROS attack in plants: a proteomics view. JOURNAL OF EXPERIMENTAL BOTANY. 2015;66(10):2935–44.
IEEE
[1]
M. S. Akter et al., “Cysteines under ROS attack in plants: a proteomics view,” JOURNAL OF EXPERIMENTAL BOTANY, vol. 66, no. 10, pp. 2935–2944, 2015.
@article{6863866,
  abstract     = {Plants generate reactive oxygen species (ROS) as part of their metabolism and in response to various external stress factors, potentially causing significant damage to biomolecules and cell structures. During the course of evolution, plants have adapted to ROS toxicity, and use ROS as signalling messengers that activate defence responses. Cysteine (Cys) residues in proteins are one of the most sensitive targets for ROS-mediated post-translational modifications, and they have become key residues for ROS signalling studies. The reactivity of Cys residues towards ROS, and their ability to react to different oxidation states, allow them to appear at the crossroads of highly dynamic oxidative events. As such, a redox-active cysteine can be present as S-glutathionylated (-SSG), disulfide bonded (S-S), sulfenylated (-SOH), sulfinylated (-SO2H), and sulfonylated (-SO3H). The sulfenic acid (-SOH) form has been considered as part of ROS-sensing pathways, as it leads to further modifications which affect protein structure and function. Redox proteomic studies are required to understand how and why cysteines undergo oxidative post-translational modifications and to identify the ROS-sensor proteins. Here, we update current knowledge of cysteine reactivity with ROS. Further, we give an overview of proteomic techniques that have been applied to identify different redox-modified cysteines in plants. There is a particular focus on the identification of sulfenylated proteins, which have the potential to be involved in plant signal transduction.},
  author       = {Akter, Mosammat Salma and Huang, Jingjing and Waszczak, Cezary and Jacques, Silke and Gevaert, Kris and Van Breusegem, Frank and Messens, Joris},
  issn         = {0022-0957},
  journal      = {JOURNAL OF EXPERIMENTAL BOTANY},
  keywords     = {REDOX REGULATION,NITRIC-OXIDE,HYDROGEN-PEROXIDE,ARABIDOPSIS-THALIANA,ACTIVE-SITE CYSTEINE,S-NITROSYLATED PROTEINS,DISULFIDE BOND FORMATION,redox proteomics,THIOREDOXIN TARGET PROTEINS,SULFENIC ACID FORMATION,sulfenic acid,GENETICALLY ENCODED PROBE,redox regulation,reactive oxygen species (ROS),oxidative post-translational modification,Cysteine (Cys)},
  language     = {eng},
  number       = {10},
  pages        = {2935--2944},
  title        = {Cysteines under ROS attack in plants: a proteomics view},
  url          = {http://dx.doi.org/10.1093/jxb/erv044},
  volume       = {66},
  year         = {2015},
}

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