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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| Asıl Yazarlar: | , , , , |
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| Materyal Türü: | Artigo |
| Dil: | Inglês |
| Baskı/Yayın Bilgisi: |
Frontiers Media S.A.
2025-03-01
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| Seri Bilgileri: | Frontiers in Plant Science |
| Konular: | |
| Online Erişim: | https://www.frontiersin.org/articles/10.3389/fpls.2025.1554272/full |
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