Related Experiment Video
Updated: Aug 8, 2025

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
Published on: June 21, 2021
Cystathionine-β-synthase X proteins negatively regulate NADPH-thioredoxin reductase C activity
Chau M Tran1, Shoko Mihara1, Keisuke Yoshida1
1Laboratory for Chemistry and Life Science, Institute of Innovative Research, Tokyo Institute of Technology, Nagatsuta-cho 4259-R1, Midori-Ku, Yokohama, 226-8503, Japan.
Abstract:
Redox regulation is a posttranslational modification based on the redox reaction of protein thiols. A small ubiquitous protein thioredoxin (Trx) plays a central role in redox regulation, but a unique redox-regulatory factor called NADPH-Trx reductase C (NTRC) is also found in plant chloroplasts and some cyanobacteria. Several important functions of NTRC have been suggested, but the mechanism for controlling NTRC activity remains undetermined. Cystathionine-β-synthase X (CBSX) proteins have been previously shown to interact with NTRC physically. Based on these observations, this study biochemically investigated the functional interaction between CBSX proteins and NTRC from Arabidopsis thaliana in vitro. Consequently, we concluded that CBSX proteins act as negative regulators of NTRC in the presence of AMP.
Insights
Cystathionine-β-synthase X (CBSX) proteins negatively regulate NADPH-Trx reductase C (NTRC) activity in plants. This interaction, observed in vitro, is dependent on the presence of AMP, revealing a novel regulatory mechanism for redox homeostasis.
Area of Science:
- Plant biochemistry
- Redox biology
- Posttranslational modifications
Background:
- Redox regulation is crucial for cellular processes, involving modifications of protein thiols.
- NADPH-Trx reductase C (NTRC) is a key redox regulator in plant chloroplasts, but its activity control is unclear.
- Cystathionine-β-synthase X (CBSX) proteins are known to interact with NTRC.
Purpose of the Study:
- To biochemically investigate the functional interaction between CBSX proteins and NTRC from Arabidopsis thaliana.
- To determine the regulatory role of CBSX proteins on NTRC activity.
Main Methods:
- In vitro biochemical assays
- Analysis of protein-protein interactions
- Enzyme activity assays
Main Results:
- CBSX proteins were confirmed to interact with NTRC.
- CBSX proteins were found to inhibit NTRC activity.
- This negative regulation by CBSX is dependent on the presence of AMP.
Conclusions:
- CBSX proteins function as negative regulators of NTRC in Arabidopsis thaliana.
- AMP is essential for the inhibitory effect of CBSX on NTRC.
- This study elucidates a novel regulatory mechanism controlling NTRC activity and redox homeostasis in plants.
Related Concept Videos
Allosteric Proteins-ATCase
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
Role of Reduced Coenzymes NADH and FADH₂
Electron Transport Chain: Complex III and IV
Redox Reactions
The Electron Transport Chain
Inhibitors of the electron transport chain
Rotenone, a widely used pesticide, prevents electron transfer from Fe-S cluster to ubiquinone or Q...
ATP Synthase: Mechanism

