Meyer, Andreas J., Riemer, Jan and Rouhier, Nicolas ORCID: 0000-0002-2036-7884 (2019). Oxidative protein folding: state-of-the-art and current avenues of research in plants. New Phytol., 221 (3). S. 1230 - 1247. HOBOKEN: WILEY. ISSN 1469-8137

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Abstract

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.

Item Type: Journal Article
Creators:
CreatorsEmailORCIDORCID Put Code
Meyer, Andreas J.UNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Riemer, JanUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Rouhier, NicolasUNSPECIFIEDorcid.org/0000-0002-2036-7884UNSPECIFIED
URN: urn:nbn:de:hbz:38-157476
DOI: 10.1111/nph.15436
Journal or Publication Title: New Phytol.
Volume: 221
Number: 3
Page Range: S. 1230 - 1247
Date: 2019
Publisher: WILEY
Place of Publication: HOBOKEN
ISSN: 1469-8137
Language: English
Faculty: Faculty of Mathematics and Natural Sciences
Divisions: Faculty of Mathematics and Natural Sciences > Department of Chemistry > Institute of Biochemistry
Subjects: no entry
Uncontrolled Keywords:
KeywordsLanguage
DISULFIDE-BOND FORMATION; MITOCHONDRIAL INTERMEMBRANE SPACE; QUIESCIN-SULFHYDRYL OXIDASE; ISOMERASE FAMILY PROTEINS; CYTOCHROME B(6)F COMPLEX; ENDOPLASMIC-RETICULUM; ARABIDOPSIS-THALIANA; GLUTATHIONE PEROXIDASES; THYLAKOID MEMBRANE; RELAY SYSTEMMultiple languages
Plant SciencesMultiple languages
Refereed: Yes
URI: http://kups.ub.uni-koeln.de/id/eprint/15747

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