Functional recoding of Chlamydomonas reinhardtii thioredoxin type-h into photosynthetic type-f by switching selectivity determinants
Thioredoxins are ubiquitous disulfide reductases folded as an α/β domain of 100-120 amino acid residues. Functional redox site is composed of a pair of cysteines in a canonical WCGPC pentapeptide exposed at the surface of thioredoxins, that reduces disulfide bonds on target proteins. Several genetic...
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| Main Authors: | Stéphane D. Lemaire, Gianluca Lombardi, Andrea Mancini, Alessandra Carbone, Julien Henri |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Frontiers Media S.A.
2025-03-01
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| Series: | Frontiers in Plant Science |
| Subjects: | |
| Online Access: | https://www.frontiersin.org/articles/10.3389/fpls.2025.1554272/full |
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