Functional recoding of <i>Chlamydomonas reinhardtii</i> thioredoxin type-h into photosynthetic type-f by switching selectivity determinants.

ABSTRACT: 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 isoforms of thioredoxins are phylogenetically classified into seven types, including type-h involved in general functions in the cytosol and type-f specifically associated to photosynthetic functions in chloroplasts. Specialization of thioredoxin function is correlated to its selectivity towards a type-dependent repertoire of protein targets. In this study, we combined biochemical and computational approaches to identify amino acid residues of photosynthetic type-f thioredoxin contributing to t

SUBMITTER: Lemaire SD 

PROVIDER: S-EPMC11922929 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature