期刊
FEBS LETTERS
卷 592, 期 18, 页码 3111-3115出版社
WILEY
DOI: 10.1002/1873-3468.13216
关键词
NADPH-dependent thioredoxin reductase C; redox-regulation; tetrapyrrole biosynthesis
资金
- Deutsche Forschungsgemeinschaft (in the SPP 1710 Thiol Switches) [DFG 936 17-1]
- Deutsche Forschungsgemeinschaft [SFB/TRR 175]
- European Regional Development Fund-co financed grant from the Spanish Ministry of Innovation and Competitiveness (MINECO) [BIO2017-85195-C2-1-P]
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 thioredoxits (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.
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