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


Journal

Biochemical and biophysical research communications
ISSN: 1090-2104
Titre abrégé: Biochem Biophys Res Commun
Pays: United States
ID NLM: 0372516

Informations de publication

Date de publication:
23 04 2023
Historique:
received: 12 02 2023
accepted: 20 02 2023
pubmed: 2 3 2023
medline: 22 3 2023
entrez: 1 3 2023
Statut: ppublish

Résumé

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.

Identifiants

pubmed: 36857899
pii: S0006-291X(23)00235-8
doi: 10.1016/j.bbrc.2023.02.055
pii:
doi:

Substances chimiques

Antioxidants 0
Arabidopsis Proteins 0
Cystathionine 375YFJ481O
Cystathionine beta-Synthase EC 4.2.1.22
Thioredoxin-Disulfide Reductase EC 1.8.1.9
Thioredoxins 52500-60-4
NTRC protein, Arabidopsis EC 1.8.1.9

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

47-52

Informations de copyright

Copyright © 2023 Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of competing interest The authors have no conflicts of interest to declare.

Auteurs

Chau M Tran (CM)

Laboratory for Chemistry and Life Science, Institute of Innovative Research, Tokyo Institute of Technology, Nagatsuta-cho 4259-R1, Midori-Ku, Yokohama, 226-8503, Japan.

Shoko Mihara (S)

Laboratory for Chemistry and Life Science, Institute of Innovative Research, Tokyo Institute of Technology, Nagatsuta-cho 4259-R1, Midori-Ku, Yokohama, 226-8503, Japan.

Keisuke Yoshida (K)

Laboratory for Chemistry and Life Science, Institute of Innovative Research, Tokyo Institute of Technology, Nagatsuta-cho 4259-R1, Midori-Ku, Yokohama, 226-8503, Japan. Electronic address: kyoshida@res.titech.ac.jp.

Toru Hisabori (T)

Laboratory for Chemistry and Life Science, Institute of Innovative Research, Tokyo Institute of Technology, Nagatsuta-cho 4259-R1, Midori-Ku, Yokohama, 226-8503, Japan. Electronic address: thisabor@res.titech.ac.jp.

Articles similaires

Arabidopsis Arabidopsis Proteins Osmotic Pressure Cytoplasm RNA, Messenger
Fragaria Light Plant Leaves Osmosis Stress, Physiological
Genome Size Genome, Plant Magnoliopsida Evolution, Molecular Arabidopsis

A molecular mechanism for bright color variation in parrots.

Roberto Arbore, Soraia Barbosa, Jindich Brejcha et al.
1.00
Animals Feathers Pigmentation Parrots Aldehyde Dehydrogenase

Classifications MeSH