Sulfotransferase 4A1 activity facilitates sulfate-dependent cellular protection to oxidative stress.
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
31 01 2022
31 01 2022
Historique:
received:
28
09
2021
accepted:
13
01
2022
entrez:
1
2
2022
pubmed:
2
2
2022
medline:
4
3
2022
Statut:
epublish
Résumé
Sulfotransferase 4A1 (SULT4A1) is an orphan member of the cytosolic SULT superfamily that contains enzymes that catalyze the sulfonation of hydrophobic drugs and hormones. SULT4A1 has been assessed through all classical SULT approaches yet no SULT activity has been reported. To ascertain SULT4A1 function and activity, we utilized Saccharomyces cerevisiae as a model system, which exhibits no endogenous SULT activity nor possesses SULT-related genes. We observed that ectopic SULT4A1 expression in yeast displays similar subcellular localization as reported in mouse neurons and observed that SULT4A1 is associated with the outer mitochondria membrane. SULT4A1 expression stimulates colony formation and protects these cells from hydrogen peroxide and metabolism-associated oxidative stress. These SULT4A1-mediated phenotypes are dependent on extracellular sulfate that is converted in yeast to PAPS, the universal sulfonate donor for SULT activity. Thus, heterologous SULT4A1 expression in yeast is correctly distributed and functional, and SULT4A1 antioxidant activity is sulfate dependent supporting the concept that SULT4A1 has sulfate-associated activity.
Identifiants
pubmed: 35102205
doi: 10.1038/s41598-022-05582-4
pii: 10.1038/s41598-022-05582-4
pmc: PMC8803991
doi:
Substances chimiques
Sulfates
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1625Subventions
Organisme : NINDS NIH HHS
ID : R21 NS116312
Pays : United States
Informations de copyright
© 2022. The Author(s).
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