Thiol Redox Regulation of Plant β-Carbonic Anhydrase
β-carbonic anhydrases (βCA) accelerate the equilibrium formation between CO<sub>2</sub> and carbonate. Two plant βCA isoforms are targeted to the chloroplast and represent abundant proteins in the range of >1% of chloroplast protein. While their function in gas exchange and photosynth...
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MDPI AG
2020-07-01
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| Online Access: | https://www.mdpi.com/2218-273X/10/8/1125 |
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| author | Anna Dreyer Alexander Schackmann Alexandre Kriznik Kamel Chibani Corinna Wesemann Lara Vogelsang André Beyer Karl-Josef Dietz |
| author_facet | Anna Dreyer Alexander Schackmann Alexandre Kriznik Kamel Chibani Corinna Wesemann Lara Vogelsang André Beyer Karl-Josef Dietz |
| author_sort | Anna Dreyer |
| collection | DOAJ |
| description | β-carbonic anhydrases (βCA) accelerate the equilibrium formation between CO<sub>2</sub> and carbonate. Two plant βCA isoforms are targeted to the chloroplast and represent abundant proteins in the range of >1% of chloroplast protein. While their function in gas exchange and photosynthesis is well-characterized in carbon concentrating mechanisms of cyanobacteria and plants with C4-photosynthesis, their function in plants with C3-photosynthesis is less clear. The presence of conserved and surface-exposed cysteinyl residues in the βCA-structure urged to the question whether βCA is subject to redox regulation. Activity measurements revealed reductive activation of βCA1, whereas oxidized βCA1 was inactive. Mutation of cysteinyl residues decreased βCA1 activity, in particular C280S, C167S, C230S, and C257S. High concentrations of dithiothreitol or low amounts of reduced thioredoxins (TRXs) activated oxidized βCA1. TRX-y1 and TRX-y2 most efficiently activated βCA1, followed by TRX-f1 and f2 and NADPH-dependent TRX reductase C (NTRC). High light irradiation did not enhance βCA activity in wildtype Arabidopsis, but surprisingly in <i>βca1</i> knockout plants, indicating light-dependent regulation. The results assign a role of βCA within the thiol redox regulatory network of the chloroplast. |
| first_indexed | 2024-03-10T18:06:31Z |
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| institution | Directory Open Access Journal |
| issn | 2218-273X |
| language | English |
| last_indexed | 2024-03-10T18:06:31Z |
| publishDate | 2020-07-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biomolecules |
| spelling | doaj.art-bc96a980444d4d07a2bee7e0cd632d502023-11-20T08:27:52ZengMDPI AGBiomolecules2218-273X2020-07-01108112510.3390/biom10081125Thiol Redox Regulation of Plant β-Carbonic AnhydraseAnna Dreyer0Alexander Schackmann1Alexandre Kriznik2Kamel Chibani3Corinna Wesemann4Lara Vogelsang5André Beyer6Karl-Josef Dietz7Department of Biochemistry and Physiology of Plants, Faculty of Biology, University of Bielefeld, 33615 Bielefeld, GermanyDepartment of Biochemistry and Physiology of Plants, Faculty of Biology, University of Bielefeld, 33615 Bielefeld, GermanyCNRS, INSERM, IBSLor, Biophysics and Structural Biology, Université de Lorraine, F-5400 Nancy, FranceDepartment of Biochemistry and Physiology of Plants, Faculty of Biology, University of Bielefeld, 33615 Bielefeld, GermanyDepartment of Biochemistry and Physiology of Plants, Faculty of Biology, University of Bielefeld, 33615 Bielefeld, GermanyDepartment of Biochemistry and Physiology of Plants, Faculty of Biology, University of Bielefeld, 33615 Bielefeld, GermanyPhysics of Supramolecular Systems and Surfaces, Faculty of Physics, Bielefeld University, 33615 Bielefeld, GermanyDepartment of Biochemistry and Physiology of Plants, Faculty of Biology, University of Bielefeld, 33615 Bielefeld, Germanyβ-carbonic anhydrases (βCA) accelerate the equilibrium formation between CO<sub>2</sub> and carbonate. Two plant βCA isoforms are targeted to the chloroplast and represent abundant proteins in the range of >1% of chloroplast protein. While their function in gas exchange and photosynthesis is well-characterized in carbon concentrating mechanisms of cyanobacteria and plants with C4-photosynthesis, their function in plants with C3-photosynthesis is less clear. The presence of conserved and surface-exposed cysteinyl residues in the βCA-structure urged to the question whether βCA is subject to redox regulation. Activity measurements revealed reductive activation of βCA1, whereas oxidized βCA1 was inactive. Mutation of cysteinyl residues decreased βCA1 activity, in particular C280S, C167S, C230S, and C257S. High concentrations of dithiothreitol or low amounts of reduced thioredoxins (TRXs) activated oxidized βCA1. TRX-y1 and TRX-y2 most efficiently activated βCA1, followed by TRX-f1 and f2 and NADPH-dependent TRX reductase C (NTRC). High light irradiation did not enhance βCA activity in wildtype Arabidopsis, but surprisingly in <i>βca1</i> knockout plants, indicating light-dependent regulation. The results assign a role of βCA within the thiol redox regulatory network of the chloroplast.https://www.mdpi.com/2218-273X/10/8/1125<i>Arabidopsis thaliana</i>carbonic anhydrasesite-directed mutagenesisthiol redox regulationthioredoxin |
| spellingShingle | Anna Dreyer Alexander Schackmann Alexandre Kriznik Kamel Chibani Corinna Wesemann Lara Vogelsang André Beyer Karl-Josef Dietz Thiol Redox Regulation of Plant β-Carbonic Anhydrase Biomolecules <i>Arabidopsis thaliana</i> carbonic anhydrase site-directed mutagenesis thiol redox regulation thioredoxin |
| title | Thiol Redox Regulation of Plant β-Carbonic Anhydrase |
| title_full | Thiol Redox Regulation of Plant β-Carbonic Anhydrase |
| title_fullStr | Thiol Redox Regulation of Plant β-Carbonic Anhydrase |
| title_full_unstemmed | Thiol Redox Regulation of Plant β-Carbonic Anhydrase |
| title_short | Thiol Redox Regulation of Plant β-Carbonic Anhydrase |
| title_sort | thiol redox regulation of plant β carbonic anhydrase |
| topic | <i>Arabidopsis thaliana</i> carbonic anhydrase site-directed mutagenesis thiol redox regulation thioredoxin |
| url | https://www.mdpi.com/2218-273X/10/8/1125 |
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