Cystathionine-β-synthase X proteins negatively regulate NADPH-thioredoxin reductase C activity

Biochem Biophys Res Commun. 2023 Apr 23:653:47-52. doi: 10.1016/j.bbrc.2023.02.055. Epub 2023 Feb 21.

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.

Keywords: 2-Cys Prx; CBSX proteins; NTRC; Redox regulation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antioxidants / metabolism
  • Arabidopsis Proteins* / metabolism
  • Arabidopsis* / metabolism
  • Chloroplasts / metabolism
  • Cystathionine / metabolism
  • Cystathionine beta-Synthase / metabolism
  • Oxidation-Reduction
  • Thioredoxin-Disulfide Reductase / metabolism
  • Thioredoxins / metabolism

Substances

  • Antioxidants
  • Arabidopsis Proteins
  • Cystathionine
  • Cystathionine beta-Synthase
  • Thioredoxin-Disulfide Reductase
  • Thioredoxins
  • NTRC protein, Arabidopsis