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Balmer Y, Koller A, Val GD, et al. Proteomics uncovers proteins interacting electrostatically with thioredoxin in chloroplasts. Photosynth Res. 2004;79(3):275-80doi: 10.1023/B:PRES.0000017207.88257.d4.
Balmer, Y., Koller, A., Val, G. D., Schürmann, P., & Buchanan, B. B. (2004). Proteomics uncovers proteins interacting electrostatically with thioredoxin in chloroplasts. Photosynthesis research, 79(3), 275-80. https://doi.org/10.1023/B:PRES.0000017207.88257.d4
Balmer, Yves, et al. "Proteomics uncovers proteins interacting electrostatically with thioredoxin in chloroplasts." Photosynthesis research vol. 79,3 (2004): 275-80. doi: https://doi.org/10.1023/B:PRES.0000017207.88257.d4
Balmer Y, Koller A, Val GD, Schürmann P, Buchanan BB. Proteomics uncovers proteins interacting electrostatically with thioredoxin in chloroplasts. Photosynth Res. 2004;79(3):275-80. doi: 10.1023/B:PRES.0000017207.88257.d4. PMID: 16328793.
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Photosynth Res. 2004;79(3):275-80. doi: 10.1023/B:PRES.0000017207.88257.d4.

Proteomics uncovers proteins interacting electrostatically with thioredoxin in chloroplasts.

Photosynthesis research

Yves Balmer, Antonius Koller, Greg Del Val, Peter Schürmann, Bob B Buchanan

Affiliations

  1. Department of Plant and Microbial Biology, University of California, 111 Koshland Hall, Berkeley, CA, 94720, USA.

PMID: 16328793 DOI: 10.1023/B:PRES.0000017207.88257.d4

Abstract

The ability of thioredoxin f to form an electrostatic (non-covalent) complex, earlier found with fructose-1,6-bisphosphatase, was extended to include 27 previously unrecognized proteins functional in 11 processes of chloroplasts. The proteins were identified by combining thioredoxin f affinity chromatography with proteomic analysis using tandem mass spectrometry. The results provide evidence that an association with thioredoxin enables the interacting protein to achieve an optimal conformation, so as to facilitate: (i) the transfer of reducing equivalents from the ferredoxin/ferredoxin-thioredoxin reductase complex to a target protein; (ii) in some cases, to enable the channeling of metabolite substrates; (iii) to function as a subunit in the formation of multienzyme complexes.

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