Plant redox proteomics
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Plant redox proteomics. / Navrot, Nicolas; Finnie, Christine; Svensson, Birte; Hägglund, Per.
I: Journal of Proteomics, Bind 74, Nr. 8, 2011, s. 1450-1462.Publikation: Bidrag til tidsskrift › Review › Forskning › fagfællebedømt
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TY - JOUR
T1 - Plant redox proteomics
AU - Navrot, Nicolas
AU - Finnie, Christine
AU - Svensson, Birte
AU - Hägglund, Per
PY - 2011
Y1 - 2011
N2 - In common with other aerobic organisms, plants are exposed to reactive oxygen species resulting in formation of post-translational modifications related to protein oxidoreduction (redox PTMs) that may inflict oxidative protein damage. Accumulating evidence also underscores the importance of redox PTMs in regulating enzymatic activities and controlling biological processes in plants. Notably, proteins controlling the cellular redox state, e.g. thioredoxin and glutaredoxin, appear to play dual roles to maintain oxidative stress resistance and regulate signal transduction pathways via redox PTMs. To get a comprehensive overview of these types of redox-regulated pathways there is therefore an emerging interest to monitor changes in redox PTMs on a proteome scale. Compared to some other PTMs, e.g. protein phosphorylation, redox PTMs have received less attention in plant proteome analysis, possibly due to technical challenges such as with maintaining the in vivo redox states of proteins and the lability of certain PTMs, e.g. nitrosylations, during sample preparation and mass spectrometric analysis. The present review article provides an overview of the recent developments in the emerging area of plant redox proteomics.
AB - In common with other aerobic organisms, plants are exposed to reactive oxygen species resulting in formation of post-translational modifications related to protein oxidoreduction (redox PTMs) that may inflict oxidative protein damage. Accumulating evidence also underscores the importance of redox PTMs in regulating enzymatic activities and controlling biological processes in plants. Notably, proteins controlling the cellular redox state, e.g. thioredoxin and glutaredoxin, appear to play dual roles to maintain oxidative stress resistance and regulate signal transduction pathways via redox PTMs. To get a comprehensive overview of these types of redox-regulated pathways there is therefore an emerging interest to monitor changes in redox PTMs on a proteome scale. Compared to some other PTMs, e.g. protein phosphorylation, redox PTMs have received less attention in plant proteome analysis, possibly due to technical challenges such as with maintaining the in vivo redox states of proteins and the lability of certain PTMs, e.g. nitrosylations, during sample preparation and mass spectrometric analysis. The present review article provides an overview of the recent developments in the emerging area of plant redox proteomics.
KW - Ascorbate
KW - Glutaredoxin
KW - Oxidative stress
KW - Reactive nitrogen species
KW - Reactive oxygen species
KW - Redox
KW - Thioredoxin
U2 - 10.1016/j.jprot.2011.03.008
DO - 10.1016/j.jprot.2011.03.008
M3 - Review
C2 - 21406256
AN - SCOPUS:79961011220
VL - 74
SP - 1450
EP - 1462
JO - Journal of Proteomics
JF - Journal of Proteomics
SN - 1874-3919
IS - 8
ER -
ID: 240160289