Publication Information
Jacques et al., 2015
Abstract
Mol Cell Proteomics. 2015 May;14(5):1217-29. doi: 10.1074/mcp.M114.043729. Epub
2015 Feb 18.
Protein Methionine Sulfoxide Dynamics in Arabidopsis thaliana under Oxidative
Stress.
Jacques S(1), Ghesquière B(2), De Bock PJ(2), Demol H(2), Wahni K(3), Willems
P(1), Messens J(3), Van Breusegem F(4), Gevaert K(5).
Author information:
(1)From the Department of Medical Protein Research, VIB, B-9000 Ghent, Belgium,
Department of Biochemistry, Ghent University, B-9000 Ghent, Belgium, Department
of Plant Systems Biology, VIB, Technologiepark 927, B-9052 Ghent, Belgium,
Department of Plant Biotechnology and Bioinformatics, Ghent University,
Technologiepark 927, B-9052 Ghent, Belgium.
(2)From the Department of Medical Protein Research, VIB, B-9000 Ghent, Belgium,
Department of Biochemistry, Ghent University, B-9000 Ghent, Belgium.
(3)VIB Structural Biology Research Center, Vrije Universiteit Brussel (VUB),
B-1050 Brussels, Belgium, Brussels Center for Redox Biology, B-1050 Brussels,
Belgium, Structural Biology Brussels, Vrije Universiteit Brussel, B-1050
Brussels, Belgium.
(4)Department of Plant Systems Biology, VIB, Technologiepark 927, B-9052 Ghent,
Belgium, Department of Plant Biotechnology and Bioinformatics, Ghent University,
Technologiepark 927, B-9052 Ghent, Belgium, frank.vanbreusegem@psb.ugent.be.
(5)From the Department of Medical Protein Research, VIB, B-9000 Ghent, Belgium,
Department of Biochemistry, Ghent University, B-9000 Ghent, Belgium,
kris.gevaert@vib-ugent.be.
Reactive oxygen species such as hydrogen peroxide can modify proteins via direct
oxidation of their sulfur-containing amino acids, cysteine and methionine.
Methionine oxidation, studied here, is a reversible posttranslational
modification that is emerging as a mechanism by which proteins perceive
oxidative stress and function in redox signaling. Identification of proteins
with oxidized methionines is the first prerequisite toward understanding the
functional effect of methionine oxidation on proteins and the biological
processes in which they are involved. Here, we describe a proteome-wide study of
in vivo protein-bound methionine oxidation in plants upon oxidative stress using
Arabidopsis thaliana catalase 2 knock-out plants as a model system. We
identified over 500 sites of oxidation in about 400 proteins and quantified the
differences in oxidation between wild-type and catalase 2 knock-out plants. We
show that the activity of two plant-specific glutathione S-transferases, GSTF9
and GSTT23, is significantly reduced upon oxidation. And, by sampling over time,
we mapped the dynamics of methionine oxidation and gained new insights into this
complex and dynamic landscape of a part of the plant proteome that is sculpted
by oxidative stress.
© 2015 by The American Society for Biochemistry and Molecular Biology, Inc.
DOI: 10.1074/mcp.M114.043729
PMCID: PMC4424394
PMID: 25693801 [Indexed for MEDLINE]
