In Vitro interaction between yeast frataxin and superoxide dismutases: Influence of mitochondrial metals.
Fast kinetics
Friedreich Ataxia
Oxidative stress
Protein docking
Journal
Biochimica et biophysica acta. General subjects
ISSN: 1872-8006
Titre abrégé: Biochim Biophys Acta Gen Subj
Pays: Netherlands
ID NLM: 101731726
Informations de publication
Date de publication:
05 2019
05 2019
Historique:
received:
02
10
2018
revised:
15
02
2019
accepted:
19
02
2019
pubmed:
25
2
2019
medline:
4
12
2019
entrez:
25
2
2019
Statut:
ppublish
Résumé
Friedreich's ataxia results from a decreased expression of the nuclear gene encoding the mitochondrial protein, frataxin. Frataxin participates in the biosynthesis of iron-sulfur clusters and heme cofactors, as well as in iron storage and protection against oxidative stress. How frataxin interacts with the antioxidant defence components is poorly understood. Therefore, we have investigated by kinetic, thermodynamic and modelling approaches the molecular interactions between yeast frataxin (Yfh1) and superoxide dismutases, Sod1 and Sod2, and the influence of Yfh1 on their enzymatic activities. Yfh1 interacts with cytosolic Sod1 with a dissociation constant, K This work confirms the participation of Yfh1 in cellular defence against oxidative stress.
Sections du résumé
BACKGROUND
Friedreich's ataxia results from a decreased expression of the nuclear gene encoding the mitochondrial protein, frataxin. Frataxin participates in the biosynthesis of iron-sulfur clusters and heme cofactors, as well as in iron storage and protection against oxidative stress. How frataxin interacts with the antioxidant defence components is poorly understood.
METHODS
Therefore, we have investigated by kinetic, thermodynamic and modelling approaches the molecular interactions between yeast frataxin (Yfh1) and superoxide dismutases, Sod1 and Sod2, and the influence of Yfh1 on their enzymatic activities.
RESULTS
Yfh1 interacts with cytosolic Sod1 with a dissociation constant, K
CONCLUSIONS
This work confirms the participation of Yfh1 in cellular defence against oxidative stress.
Identifiants
pubmed: 30797804
pii: S0304-4165(19)30045-5
doi: 10.1016/j.bbagen.2019.02.011
pii:
doi:
Substances chimiques
Iron-Binding Proteins
0
Metals, Heavy
0
Superoxide Dismutase
EC 1.15.1.1
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
883-892Informations de copyright
Copyright © 2019 Elsevier B.V. All rights reserved.