Redox-control of chlorophyll biosynthesis mainly depends on thioredoxins.
In order to maintain enzyme stability and activity, chloroplasts use two systems of thiol-disulfide reductases for the control of redox-dependent properties of proteins. Previous studies have revealed that plastid-localized thioredoxins (TRX) and the NADPH-dependent thioredoxin reductase C (NTRC) are important for the reduction of cysteine residues of enzymes involved in chlorophyll synthesis. Very recently, it was shown that the pale green phenotype of the ntrc mutant is suppressed when the contents of 2-cysteine peroxiredoxins (2CP) A and B are decreased. Here, we show that suppression of the ntrc phenotype results from a recovery of wild-type-like redox control of chlorophyll biosynthesis enzymes in ntrc/2cp mutants. The presented results support the conclusion that TRXs rather than NTRC are the predominant reductases mediating the redox-regulation of these enzymes.
['Richter|Andreas S|AS|0000-0002-2293-7297', 'Pérez-Ruiz|Juan M|JM|', 'Cejudo|Francisco Javier|FJ|', 'Grimm|Bernhard|B|']
D017360:Arabidopsis D029681:Arabidopsis Proteins D002734:Chlorophyll D002736:Chloroplasts D008027:Light D009154:Mutation D010788:Photosynthesis D036226:Seedlings D013880:Thioredoxin-Disulfide Reductase D013879:Thioredoxins
NADPH-dependent thioredoxin reductase C redox-regulation tetrapyrrole biosynthesis