The dynamic thiol-disulphide redox proteome of the Arabidopsis thaliana chloroplast as revealed by differential electrophoretic mobility
Stroeher E, Dietz K-J (2008)
PHYSIOLOGIA PLANTARUM 133(3): 566-583.
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Autor*in
Stroeher, Elke;
Dietz, Karl-JosefUniBi
Einrichtung
Abstract / Bemerkung
The dynamics of the thiol-disulphide redox proteome is central to cell function and its regulation. Altered mobility of proteins in the oxidized and reduced state allows the MS-based identification of those thiol-disulphide proteins that undergo major conformational changes. A proteomic approach was taken with thylakoid-bound, luminal and ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco)-less stromal subproteome fractions of the chloroplast from Arabidopsis thaliana. Among the 49 verified polypeptides were 22 novel redox proteins, previously not reported as being part of the redox proteome. Among the redox-affected proteins were PsbA (D1), PsaA1 and PsaF, chloroplast monodehydroascorbate reductase and also the Deg1 protease. Recombinant Deg1 and Deg2 revealed redox dependence of their proteolytic activity. The data provide new insights into the redox network of the chloroplast.
Erscheinungsjahr
2008
Zeitschriftentitel
PHYSIOLOGIA PLANTARUM
Band
133
Ausgabe
3
Seite(n)
566-583
ISSN
0031-9317
eISSN
1399-3054
Page URI
https://pub.uni-bielefeld.de/record/1587349
Zitieren
Stroeher E, Dietz K-J. The dynamic thiol-disulphide redox proteome of the Arabidopsis thaliana chloroplast as revealed by differential electrophoretic mobility. PHYSIOLOGIA PLANTARUM. 2008;133(3):566-583.
Stroeher, E., & Dietz, K. - J. (2008). The dynamic thiol-disulphide redox proteome of the Arabidopsis thaliana chloroplast as revealed by differential electrophoretic mobility. PHYSIOLOGIA PLANTARUM, 133(3), 566-583. https://doi.org/10.1111/j.1399-3054.2008.01103.x
Stroeher, Elke, and Dietz, Karl-Josef. 2008. “The dynamic thiol-disulphide redox proteome of the Arabidopsis thaliana chloroplast as revealed by differential electrophoretic mobility”. PHYSIOLOGIA PLANTARUM 133 (3): 566-583.
Stroeher, E., and Dietz, K. - J. (2008). The dynamic thiol-disulphide redox proteome of the Arabidopsis thaliana chloroplast as revealed by differential electrophoretic mobility. PHYSIOLOGIA PLANTARUM 133, 566-583.
Stroeher, E., & Dietz, K.-J., 2008. The dynamic thiol-disulphide redox proteome of the Arabidopsis thaliana chloroplast as revealed by differential electrophoretic mobility. PHYSIOLOGIA PLANTARUM, 133(3), p 566-583.
E. Stroeher and K.-J. Dietz, “The dynamic thiol-disulphide redox proteome of the Arabidopsis thaliana chloroplast as revealed by differential electrophoretic mobility”, PHYSIOLOGIA PLANTARUM, vol. 133, 2008, pp. 566-583.
Stroeher, E., Dietz, K.-J.: The dynamic thiol-disulphide redox proteome of the Arabidopsis thaliana chloroplast as revealed by differential electrophoretic mobility. PHYSIOLOGIA PLANTARUM. 133, 566-583 (2008).
Stroeher, Elke, and Dietz, Karl-Josef. “The dynamic thiol-disulphide redox proteome of the Arabidopsis thaliana chloroplast as revealed by differential electrophoretic mobility”. PHYSIOLOGIA PLANTARUM 133.3 (2008): 566-583.
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The extrinsic proteins of Photosystem II.
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Impairment of the photorespiratory pathway accelerates photoinhibition of photosystem II by suppression of repair but not acceleration of damage processes in Arabidopsis.
Takahashi S, Bauwe H, Badger M., Plant Physiol. 144(1), 2007
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The structure of a plant photosystem I supercomplex at 3.4 A resolution.
Amunts A, Drory O, Nelson N., Nature 447(7140), 2007
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S-glutathionylation in protein redox regulation.
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The E3 ligase AtCHIP ubiquitylates FtsH1, a component of the chloroplast FtsH protease, and affects protein degradation in chloroplasts.
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Appearance of Glutathione during the Early Stages of the Germination of Seeds
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