The oxidative protein folding machinery in plant cells
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REVIEW ARTICLE
The oxidative protein folding machinery in plant cells Isabel Aller & Andreas J. Meyer
Received: 20 September 2012 / Accepted: 2 October 2012 / Published online: 23 October 2012 # Springer-Verlag Wien 2012
Abstract Formation of intra-molecular disulfides and concomitant oxidative protein folding is essential for stability and catalytic function of many soluble and membrane-bound proteins in the endomembrane system, the mitochondrial intermembrane space and the thylakoid lumen. Disulfide generation from free cysteines in nascent polypeptide chains is generally a catalysed process for which distinct pathways exist in all compartments. A high degree of similarities between highly diverse eukaryotic and bacterial systems for generation of protein disulfides indicates functional conservation of key processes throughout evolution. However, while many aspects about molecular function of enzymatic systems promoting disulfide formation have been demonstrated for bacterial and non-plant eukaryotic organisms, it is now clear that the plant machinery for oxidative protein folding displays distinct details, suggesting that the different pathways have been adapted to plant-specific requirements in terms of compartmentation, molecular function and regulation. Here, we aim to evaluate biological diversity by comparing the plant systems for oxidative protein folding to the respective systems from non-plant eukaryotes. Keywords ER thiol oxidase . Oxidative protein folding . Protein disulfide isomerase . Thiol-disulfide relay . Quiescin sulfhydryl oxidase . Vitamin K epoxide reductase Abbreviations CCS1 Chaperone for copper/zinc superoxide dismutase 1 CSD1 Copper/zinc superoxide dismutase 1 EGSH Glutathione redox potential Handling Editor: David Robinson I. Aller : A. J. Meyer (*) INRES—Chemical Signalling, University of Bonn, Friedrich-Ebert-Allee 144, D-53113 Bonn, Germany e-mail: [email protected]
ERO ERV FAD GPX GR GSH GSSG IMS LRR MIA40 PDI PRX QSOX RALF TMD UPR VKOR
Endoplasmic reticulum thiol oxidase Essential for respiration and viability Flavin adenine dinucleotide Glutathione peroxidase Glutathione reductase Reduced glutathione Glutathione disulfide Inter-membrane space Leucine-rich repeat Mitochondrial IMS import and assembly pathway 40 kDa Protein disulfide isomerase Peroxiredoxin Quiescin sulfhydryl oxidase Rapid alkalinisation factor Transmembrane domain Unfolded protein response Vitamin K epoxide reductase
Introduction Formation of intra-molecular disulfide bonds is a frequently observed process in all cellular compartments. However, in the cytosol, the chloroplast stroma, the mitochondrial matrix and peroxisomes, the redox environment is highly reducing (Meyer et al. 2007; Schwarzländer et al. 2008). Thus, formation of disulfides is usually transitory. Such transitory disulfides can be exploited as thiol switches for regulatory processes during plant adaptation to normal diurnal environmental changes such as dark–light cycle as well as for thiol switches sensing oxidative challenges during s
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