Operation of trans-thylakoid thiol-metabolizing pathways in photosynthesis

Karamoko, Mohamed; Gabilly, Stéphane T.; Hamel, Patrice

doi:10.3389/fpls.2013.00476

Cited by 22 publications

(19 citation statements)

References 62 publications

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“…The FKBP13 results have been extended in a recent study to violaxanthin de-epoxidase, another resident of the lumen (129). This and related research (82,89) opens the door to a largely unexplored field encompassing enzymes such as those engaged in photosystem II supercomplex formation. Amparo Lima, an adept graduate student, was central to the photosystem II immunophilin work (89).…”

Section: Redox Regulation Across Membranesmentioning

confidence: 95%

The Path to Thioredoxin and Redox Regulation in Chloroplasts

Buchanan

2016

Annu. Rev. Plant Biol.

114

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After a brief discussion of my graduate work at Duke University, I describe a series of investigations on redox proteins at the University of California, Berkeley. Starting with ferredoxin from fermentative bacteria, the Berkeley research fostered experiments that uncovered a pathway for fixing CO 2 in bacterial photosynthesis. The carbon work, in turn, opened new vistas, including the discovery that thioredoxin functions universally in regulating the Calvin-Benson cycle in oxygenic photosynthesis. These experiments, which took place over a 50-year period, led to the formulation of a set of biological principles and set the stage for research demonstrating a role for redox in the regulation of previously unrecognized processes extending far beyond photosynthesis.

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Section: Redox Regulation Across Membranesmentioning

confidence: 95%

The Path to Thioredoxin and Redox Regulation in Chloroplasts

Buchanan

2016

Annu. Rev. Plant Biol.

114

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“…The critical role of LTO1 for plant growth, and PSII assembly and function indicates that its targets are important proteins. In thylakoids, many proteins with disulfide bonds have been detected (Karamoko et al ., ). Proteomic analysis has identified different potential targets of LTO1 by either yeast two‐hybrid analysis or proteomics on whole cells comparing WT and lto1 plants (Lu et al ., , ).…”

Section: Disulfide Bond Formation On Luminal Proteins In Thylakoidsmentioning

confidence: 99%

Oxidative protein folding: state‐of‐the‐art and current avenues of research in plants

2018

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Contents Summary I. Introduction II. Formation and isomerization of disulfides in the ER and the Golgi apparatus III. The disulfide relay in the mitochondrial intermembrane space: why are plants different? IV. Disulfide bond formation on luminal proteins in thylakoids V. Conclusion Acknowledgements References 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.

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“…Thiol/disulfide modulation is important for regulating photosynthetic processes (Järvi et al, 2013 ; Karamoko et al, 2013 ). Three types of thiol/disulfide-modulating proteins have been found to be involved in the assembly, stability, function, and repair of PSII: protein disulfide isomerases (PDIases), protein disulfide reducing proteins, and protein thiol oxidizing proteins.…”

Section: Proteins That Influence the Assembly Stability And Repair mentioning

confidence: 99%

Identification and Roles of Photosystem II Assembly, Stability, and Repair Factors in Arabidopsis

2016

Front. Plant Sci.

130

117

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Photosystem II (PSII) is a multi-component pigment-protein complex that is responsible for water splitting, oxygen evolution, and plastoquinone reduction. Components of PSII can be classified into core proteins, low-molecular-mass proteins, extrinsic oxygen-evolving complex (OEC) proteins, and light-harvesting complex II proteins. In addition to these PSII subunits, more than 60 auxiliary proteins, enzymes, or components of thylakoid protein trafficking/targeting systems have been discovered to be directly or indirectly involved in de novo assembly and/or the repair and reassembly cycle of PSII. For example, components of thylakoid-protein-targeting complexes and the chloroplast-vesicle-transport system were found to deliver PSII subunits to thylakoid membranes. Various auxiliary proteins, such as PsbP-like (Psb stands for PSII) and light-harvesting complex-like proteins, atypical short-chain dehydrogenase/reductase family proteins, and tetratricopeptide repeat proteins, were discovered to assist the de novo assembly and stability of PSII and the repair and reassembly cycle of PSII. Furthermore, a series of enzymes were discovered to catalyze important enzymatic steps, such as C-terminal processing of the D1 protein, thiol/disulfide-modulation, peptidylprolyl isomerization, phosphorylation and dephosphorylation of PSII core and antenna proteins, and degradation of photodamaged PSII proteins. This review focuses on the current knowledge of the identities and molecular functions of different types of proteins that influence the assembly, stability, and repair of PSII in the higher plant Arabidopsis thaliana.

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Operation of trans-thylakoid thiol-metabolizing pathways in photosynthesis

Cited by 22 publications

References 62 publications

The Path to Thioredoxin and Redox Regulation in Chloroplasts

The Path to Thioredoxin and Redox Regulation in Chloroplasts

Oxidative protein folding: state‐of‐the‐art and current avenues of research in plants

Identification and Roles of Photosystem II Assembly, Stability, and Repair Factors in Arabidopsis

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