Flexibility of Oxidized and Reduced States of the Chloroplast Regulatory Protein CP12 in Isolation and in Cell Extracts
Abstract
:1. Introduction
2. Materials and Methods
2.1. Amide-Water Proton Exchange Kinetic Measurements by NMR
2.2. Gibbs Free Energy Derived from Protection Factors
2.3. Amide–Water Proton Exchange Kinetic Measurements by MS
2.4. Temperature Dependence of the NMR Chemical Shift and Signal Intensity
2.5. Thermodynamic of the Redox Transition
2.6. Monitoring the Kinetic of Oxidation
2.7. Monitoring of the Kinetic of Reduction
2.8. Cell Extract Preparation
2.9. Diffusion Coefficient Determination
2.10. Determination of ΔG of Binding
3. Results
3.1. Structural Transition of the Region Encompassing the C66–C75 Disulfide Bridge upon Oxidation of the Isolated Protein
3.2. Structural Transition of the Region Encompassing the C23–C31 Disulfide Bridge upon Oxidation of the Isolated Protein
3.3. Structural Properties of CP12red in the Presence of C. reinhardtii Cell Extract
3.4. Structural Properties of the C66–C75 Disulfide Bridge in CP12ox in the Presence of C. reinhardtii Cell Extract
3.5. Thermodynamical Properties of the Redox Transition of Both Disulfide Bridges in Isolated CP12
3.6. Rate of Oxidation and Reduction of Both Disulfide Bridges in Isolated CP12
3.7. Reversible Redox Transition of CP12 in the Presence of C. reinhardtii Cell Extract
4. Discussion
4.1. Isolated CP12red Is Intrinsically Disordered
4.2. The Two Disulfide Bridges Are in Regions with Distinct Structural Properties in Isolated CP12ox
4.3. The Distinct Regions of CP12ox Differ in Structural Dynamics and in Affinity for Their Interacting Partners
4.4. Thermodynamically Independent and Reversible Redox Transition of Both Disulfide Bridges in CP12
4.5. Asynchrony of the Reduction of the Two Disulfide Bridges, Synchrony of Their Formation
4.6. Effect of Cell Extract on Nter-CP12 and Cter-CP12
5. Conclusions
Supplementary Materials
Author Contributions
Funding
Institutional Review Board Statement
Informed Consent Statement
Data Availability Statement
Acknowledgments
Conflicts of Interest
References
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Launay, H.; Shao, H.; Bornet, O.; Cantrelle, F.-X.; Lebrun, R.; Receveur-Brechot, V.; Gontero, B. Flexibility of Oxidized and Reduced States of the Chloroplast Regulatory Protein CP12 in Isolation and in Cell Extracts. Biomolecules 2021, 11, 701. https://doi.org/10.3390/biom11050701
Launay H, Shao H, Bornet O, Cantrelle F-X, Lebrun R, Receveur-Brechot V, Gontero B. Flexibility of Oxidized and Reduced States of the Chloroplast Regulatory Protein CP12 in Isolation and in Cell Extracts. Biomolecules. 2021; 11(5):701. https://doi.org/10.3390/biom11050701
Chicago/Turabian StyleLaunay, Helene, Hui Shao, Olivier Bornet, Francois-Xavier Cantrelle, Regine Lebrun, Veronique Receveur-Brechot, and Brigitte Gontero. 2021. "Flexibility of Oxidized and Reduced States of the Chloroplast Regulatory Protein CP12 in Isolation and in Cell Extracts" Biomolecules 11, no. 5: 701. https://doi.org/10.3390/biom11050701