Oxidative protein folding

Autor: Meyer, Andreas J, Riemer, Jan, Rouhier, Nicolas
Přispěvatelé: University of Bonn, University of Cologne, Interactions Arbres-Microorganismes (IAM), Université de Lorraine (UL)-Institut National de la Recherche Agronomique (INRA), French National Research Agency (ANR) ANR-11-LABX-0002-01, Deutsche Forschungsgemeinschaft (DFG) within the Research Training Group GRK 2064, Priority Program SPP1710 ME1567/9-1/2, DFG (Priority Program SPP1710) RI2150/2-2, Institut National de la Recherche Agronomique (INRA)-Université de Lorraine (UL)
Jazyk: angličtina
Rok vydání: 2019
Předmět:
Zdroj: New Phytologist
New Phytologist, Wiley, 2019, 221 (3), pp.1230-1246. ⟨10.1111/nph.15436⟩
ISSN: 0028-646X
1469-8137
DOI: 10.1111/nph.15436⟩
Popis: Disulfide bond formation on luminal proteins in thylakoids 1240 V. Conclusion 1242 Acknowledgements 1242 References 1242 SUMMARY: Disulfide bonds are post-translational modifications crucial for the structure and function of thousands of proteins. Their formation and isomerization, referred to as oxidative folding, require specific protein machineries found in oxidizing subcellular compartments, namely the endoplasmic reticulum and the associated endomembrane system, the intermembrane space of mitochondria and the thylakoid lumen of chloroplasts. At least one protein component is required for transferring electrons from substrate proteins to an acceptor that is usually molecular oxygen. For oxidation reactions, incoming reduced substrates are oxidized by thiol-oxidoreductase proteins (or domains in case of chimeric proteins), which are usually themselves oxidized by a single thiol oxidase, the enzyme generating disulfide bonds de novo. By contrast, the description of the molecular actors and pathways involved in proofreading and isomerization of misfolded proteins, which require a tightly controlled redox balance, lags behind. Herein we provide a general overview of the knowledge acquired on the systems responsible for oxidative protein folding in photosynthetic organisms, highlighting their particularities compared to other eukaryotes. Current research challenges are discussed including the importance and specificity of these oxidation systems in the context of the existence of reducing systems in the same compartments.
Databáze: OpenAIRE
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