Cysteines under ROS attack in plants: a proteomics view.
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.
Department of Plant Systems Biology, VIB, 9052 Ghent, Belgium Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium Structural Biology Research Centre, VIB, 1050 Brussels, Belgium Brussels Centre for Redox Biology, 1050 Brussels, Belgium Structural Biology Brussels, Vrije Universiteit Brussel, 1050 Brussels, Belgium Faculty of Biological Sciences, University of Dhaka, 1000 Dhaka, Bangladesh.
Salma
S
Akter
Structural Biology Research Centre, VIB, 1050 Brussels, Belgium Brussels Centre for Redox Biology, 1050 Brussels, Belgium Structural Biology Brussels, Vrije Universiteit Brussel, 1050 Brussels, Belgium.
Jingjing
J
Huang
Department of Plant Systems Biology, VIB, 9052 Ghent, Belgium Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium Structural Biology Research Centre, VIB, 1050 Brussels, Belgium Brussels Centre for Redox Biology, 1050 Brussels, Belgium Structural Biology Brussels, Vrije Universiteit Brussel, 1050 Brussels, Belgium.
Cezary
C
Waszczak
Department of Plant Systems Biology, VIB, 9052 Ghent, Belgium Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium Department of Medical Protein Research, VIB, 9000 Gent, Belgium Department of Biochemistry, Ghent University, 9000 Gent, Belgium.
Silke
S
Jacques
Department of Medical Protein Research, VIB, 9000 Gent, Belgium Department of Biochemistry, Ghent University, 9000 Gent, Belgium.
Kris
K
Gevaert
Department of Plant Systems Biology, VIB, 9052 Ghent, Belgium Department of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium joris.messens@vib-vub.be frank.vanbreusegem@psb.vib-ugent.be.
Frank
F
Van Breusegem
Structural Biology Research Centre, VIB, 1050 Brussels, Belgium Brussels Centre for Redox Biology, 1050 Brussels, Belgium Structural Biology Brussels, Vrije Universiteit Brussel, 1050 Brussels, Belgium joris.messens@vib-vub.be frank.vanbreusegem@psb.vib-ugent.be.
Joris
J
Messens
D003545:Cysteine / Q000378:metabolism*; D010084:Oxidation-Reduction; D018521:Plant Physiological Phenomena; D010940:Plant Proteins / Q000378:metabolism*; D020543:Proteome; D017382:Reactive Oxygen Species / Q000378:metabolism*; D015398:Signal Transduction
D010940:Plant Proteins; D020543:Proteome; D017382:Reactive Oxygen Species; D003545:Cysteine
Cysteine (Cys); oxidative post-translational modification; reactive oxygen species (ROS); redox proteomics; redox regulation; sulfenic acid.