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Updated: Feb 2, 2026

Isolation and Characterization of Intact Phycobilisome in Cyanobacteria
Published on: November 10, 2021
Characterization of TrxC, an Atypical Thioredoxin Exclusively Present in Cyanobacteria
Luis López-Maury1, Luis G Heredia-Martínez2, Francisco J Florencio3
1Instituto de Bioquímica Vegetal y Fotosíntesis, Universidad de Sevilla-CSIC, Av/Américo Vespucio 49, E-41092 Sevilla, Spain. llopez1@us.es.
Abstract:
Cyanobacteria form a diverse group of oxygenic photosynthetic prokaryotes considered to be the antecessor of plant chloroplast. They contain four different thioredoxins isoforms, three of them corresponding to m, x and y type present in plant chloroplast, while the fourth one (named TrxC) is exclusively found in cyanobacteria. TrxC has a modified active site (WCGLC) instead of the canonical (WCGPC) present in most thioredoxins. We have purified it and assayed its activity but surprisingly TrxC lacked all the classical activities, such as insulin precipitation or activation of the fructose-1,6-bisphosphatase. Mutants lacking trxC or over-expressing it were generated in the model cyanobacterium Synechocystis sp. PCC 6803 and their phenotypes have been analyzed. The ΔtrxC mutant grew at similar rates to WT in all conditions tested although it showed an increased carotenoid content especially under low carbon conditions. Overexpression strains showed reduced growth under the same conditions and accumulated lower amounts of carotenoids. They also showed lower oxygen evolution rates at high light but higher Fv'/Fm' and Non-photochemical-quenching (NPQ) in dark adapted cells, suggesting a more oxidized plastoquinone pool. All these data suggest that TrxC might have a role in regulating photosynthetic adaptation to low carbon and/or high light conditions.
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