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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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.
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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.
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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84 References

Data provided by Europe PubMed Central.

Oxidative modifications to cellular components in plants.
Moller IM, Jensen PE, Hansson A., Annu Rev Plant Biol 58(), 2007
PMID: 17288534
DNA binding and partial nucleoid localization of the chloroplast stromal enzyme ferredoxin:sulfite reductase.
Sekine K, Fujiwara M, Nakayama M, Takao T, Hase T, Sato N., FEBS J. 274(8), 2007
PMID: 17371503
The structure of a plant photosystem I supercomplex at 3.4 A resolution.
Amunts A, Drory O, Nelson N., Nature 447(7140), 2007
PMID: 17476261
S-glutathionylation in protein redox regulation.
Dalle-Donne I, Rossi R, Giustarini D, Colombo R, Milzani A., Free Radic. Biol. Med. 43(6), 2007
PMID: 17697933
Appearance of Glutathione during the Early Stages of the Germination of Seeds
HOPKINS, Nature 152(3854), 1943

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