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Sökning: swepub > Umeå universitet > Samuelsson Göran 1951 > (2005-2009) > Engelska

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1.
  • Nikitina, Julia, et al. (författare)
  • Importance of a single disulfide bond for the PsbO protein of photosystem II : protein structure stability and soluble overexpression in Escherichia coli.
  • 2008
  • Ingår i: Photosynthesis Research. - 0166-8595. ; 98, s. 391-403
  • Tidskriftsartikel (refereegranskat)abstract
    • PsbO protein is an important constituent of the water–oxidizing complex, located on the lumenal side of photosystem II. We report here the efficient expression of the spinach PsbO in E. coli where the solubility depends entirely on the formation of the disulfide bond. The PsbO protein purified from a pET32 system that includes thioredoxin fusion is properly folded and functionally active. Urea unfolding experiments imply that the reduction of the single disulfide bridge decreases stability of the protein. Analysis of inter-residue contact density through the PsbO molecule shows that Cys51 is located in a cluster with high contact density. Reduction of the Cys28–Cys51 bond is proposed to perturb the packing interactions in this cluster and destabilize the protein as a whole. Taken together, our results give evidence that PsbO exists in solution as a compact highly ordered structure, provided that the disulfide bridge is not reduced.
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2.
  • Rouhier, Nicolas, et al. (författare)
  • Identification of plant glutaredoxin targets
  • 2005
  • Ingår i: Antioxidants and Redox Signaling. - Larchmont, NY : Mary Ann Liebert. - 1523-0864. ; 7:7-8, s. 919-929
  • Tidskriftsartikel (refereegranskat)abstract
    • Glutaredoxins (Grxs) are small ubiquitous proteins of the thioredoxin (Trx) family, which catalyze dithiol–disulfide exchange reactions or reduce protein-mixed glutathione disulfides. In plants, several Trx-interacting proteins have been isolated from different compartments, whereas very few Grx-interacting proteins are known. We describe here the determination of Grx target proteins using a mutated poplar Grx, various tissular and subcellular plant extracts, and liquid chromatography coupled to tandem mass spectrometry detection. We have identified 94 putative targets, involved in many processes, including oxidative stress response [peroxiredoxins (Prxs), ascorbate peroxidase, catalase], nitrogen, sulfur, and carbon metabolisms (methionine synthase, alanine aminotransferase, phosphoglycerate kinase), translation (elongation factors E and Tu), or protein folding (heat shock protein 70). Some of these proteins were previously found to interact with Trx or to be glutathiolated in other organisms, but others could be more specific partners of Grx. To substantiate further these data, Grx was shown to support catalysis of the stroma β-type carbonic anhydrase and Prx IIF of Arabidopsis thaliana, but not of poplar 2-Cys Prx. Overall, these data suggest that the interaction could occur randomly either with exposed cysteinyl disulfide bonds formed within or between target proteins or with mixed disulfides between a protein thiol and glutathione.
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