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Calredoxin regulates the chloroplast NADPH-dependent thioredoxin reductase in Chlamydomonas reinhardtii

Calredoxin (CRX) is a calcium (Ca(2+))-dependent thioredoxin (TRX) in the chloroplast of Chlamydomonas (Chlamydomonas reinhardtii) with a largely unclear physiological role. We elucidated the CRX functionality by performing in-depth quantitative proteomics of wild-type cells compared with a crx inse...

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Autores principales: Zinzius, Karen, Marchetti, Giulia Maria, Fischer, Ronja, Milrad, Yuval, Oltmanns, Anne, Kelterborn, Simon, Yacoby, Iftach, Hegemann, Peter, Scholz, Martin, Hippler, Michael
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10602609/
https://www.ncbi.nlm.nih.gov/pubmed/37474113
http://dx.doi.org/10.1093/plphys/kiad426
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author Zinzius, Karen
Marchetti, Giulia Maria
Fischer, Ronja
Milrad, Yuval
Oltmanns, Anne
Kelterborn, Simon
Yacoby, Iftach
Hegemann, Peter
Scholz, Martin
Hippler, Michael
author_facet Zinzius, Karen
Marchetti, Giulia Maria
Fischer, Ronja
Milrad, Yuval
Oltmanns, Anne
Kelterborn, Simon
Yacoby, Iftach
Hegemann, Peter
Scholz, Martin
Hippler, Michael
author_sort Zinzius, Karen
collection PubMed
description Calredoxin (CRX) is a calcium (Ca(2+))-dependent thioredoxin (TRX) in the chloroplast of Chlamydomonas (Chlamydomonas reinhardtii) with a largely unclear physiological role. We elucidated the CRX functionality by performing in-depth quantitative proteomics of wild-type cells compared with a crx insertional mutant (IM(crx)), two CRISPR/Cas9 KO mutants, and CRX rescues. These analyses revealed that the chloroplast NADPH-dependent TRX reductase (NTRC) is co-regulated with CRX. Electron transfer measurements revealed that CRX inhibits NADPH-dependent reduction of oxidized chloroplast 2-Cys peroxiredoxin (PRX1) via NTRC and that the function of the NADPH-NTRC complex is under strict control of CRX. Via non-reducing SDS-PAGE assays and mass spectrometry, our data also demonstrated that PRX1 is more oxidized under high light (HL) conditions in the absence of CRX. The redox tuning of PRX1 and control of the NADPH-NTRC complex via CRX interconnect redox control with active photosynthetic electron transport and metabolism, as well as Ca(2+) signaling. In this way, an economic use of NADPH for PRX1 reduction is ensured. The finding that the absence of CRX under HL conditions severely inhibited light-driven CO(2) fixation underpins the importance of CRX for redox tuning, as well as for efficient photosynthesis.
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spelling pubmed-106026092023-10-27 Calredoxin regulates the chloroplast NADPH-dependent thioredoxin reductase in Chlamydomonas reinhardtii Zinzius, Karen Marchetti, Giulia Maria Fischer, Ronja Milrad, Yuval Oltmanns, Anne Kelterborn, Simon Yacoby, Iftach Hegemann, Peter Scholz, Martin Hippler, Michael Plant Physiol Research Article Calredoxin (CRX) is a calcium (Ca(2+))-dependent thioredoxin (TRX) in the chloroplast of Chlamydomonas (Chlamydomonas reinhardtii) with a largely unclear physiological role. We elucidated the CRX functionality by performing in-depth quantitative proteomics of wild-type cells compared with a crx insertional mutant (IM(crx)), two CRISPR/Cas9 KO mutants, and CRX rescues. These analyses revealed that the chloroplast NADPH-dependent TRX reductase (NTRC) is co-regulated with CRX. Electron transfer measurements revealed that CRX inhibits NADPH-dependent reduction of oxidized chloroplast 2-Cys peroxiredoxin (PRX1) via NTRC and that the function of the NADPH-NTRC complex is under strict control of CRX. Via non-reducing SDS-PAGE assays and mass spectrometry, our data also demonstrated that PRX1 is more oxidized under high light (HL) conditions in the absence of CRX. The redox tuning of PRX1 and control of the NADPH-NTRC complex via CRX interconnect redox control with active photosynthetic electron transport and metabolism, as well as Ca(2+) signaling. In this way, an economic use of NADPH for PRX1 reduction is ensured. The finding that the absence of CRX under HL conditions severely inhibited light-driven CO(2) fixation underpins the importance of CRX for redox tuning, as well as for efficient photosynthesis. Oxford University Press 2023-07-20 /pmc/articles/PMC10602609/ /pubmed/37474113 http://dx.doi.org/10.1093/plphys/kiad426 Text en © The Author(s) 2023. Published by Oxford University Press on behalf of American Society of Plant Biologists. https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Zinzius, Karen
Marchetti, Giulia Maria
Fischer, Ronja
Milrad, Yuval
Oltmanns, Anne
Kelterborn, Simon
Yacoby, Iftach
Hegemann, Peter
Scholz, Martin
Hippler, Michael
Calredoxin regulates the chloroplast NADPH-dependent thioredoxin reductase in Chlamydomonas reinhardtii
title Calredoxin regulates the chloroplast NADPH-dependent thioredoxin reductase in Chlamydomonas reinhardtii
title_full Calredoxin regulates the chloroplast NADPH-dependent thioredoxin reductase in Chlamydomonas reinhardtii
title_fullStr Calredoxin regulates the chloroplast NADPH-dependent thioredoxin reductase in Chlamydomonas reinhardtii
title_full_unstemmed Calredoxin regulates the chloroplast NADPH-dependent thioredoxin reductase in Chlamydomonas reinhardtii
title_short Calredoxin regulates the chloroplast NADPH-dependent thioredoxin reductase in Chlamydomonas reinhardtii
title_sort calredoxin regulates the chloroplast nadph-dependent thioredoxin reductase in chlamydomonas reinhardtii
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10602609/
https://www.ncbi.nlm.nih.gov/pubmed/37474113
http://dx.doi.org/10.1093/plphys/kiad426
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