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
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

1625

Subventions

Organisme : NINDS NIH HHS
ID : R21 NS116312
Pays : United States

Informations de copyright

© 2022. The Author(s).

Références

Drug Metab Dispos. 2014 May;42(5):947-53
pubmed: 24553382
Drug Metab Dispos. 2015 Jul;43(7):1037-44
pubmed: 25934576
J Biochem. 1988 Sep;104(3):362-7
pubmed: 2467904
Exp Cell Res. 2012 Jul 1;318(11):1193-200
pubmed: 22480867
FASEB J. 1997 Mar;11(4):206-16
pubmed: 9068609
Biochim Biophys Acta. 2011 Jun;1807(6):568-76
pubmed: 20804724
Drug Metab Dispos. 2019 Sep;47(9):949-953
pubmed: 31266751
Drug Metab Dispos. 2019 Mar;47(3):314-319
pubmed: 30606728
J Biol Chem. 2015 Mar 6;290(10):6203-14
pubmed: 25609251
Cell Metab. 2014 Jan 7;19(1):4-5
pubmed: 24411936
Int J Biochem Cell Biol. 2008;40(12):2686-91
pubmed: 18248844
J Bacteriol. 1993 Sep;175(17):5469-76
pubmed: 8366032
Psychiatr Genet. 2009 Feb;19(1):53-5
pubmed: 19125109
PLoS One. 2011 Apr 26;6(4):e19191
pubmed: 21541279
Hum Genet. 2014 Jul;133(7):847-59
pubmed: 24481935
J Mol Biol. 2019 May 3;431(10):2050-2059
pubmed: 30905713
PLoS One. 2014 Jul 02;9(7):e101520
pubmed: 24988429
Mol Syndromol. 2012 Apr;2(3-5):186-201
pubmed: 22670140
Psychiatr Genet. 2007 Oct;17(5):292-8
pubmed: 17728668
J Histochem Cytochem. 2003 Dec;51(12):1655-64
pubmed: 14623933
Schizophr Res. 2008 Dec;106(2-3):258-64
pubmed: 18823757
Biomolecules. 2020 Nov 06;10(11):
pubmed: 33171978
Drug Metab Dispos. 2018 Jun;46(6):860-864
pubmed: 29626075
Am J Med Genet B Neuropsychiatr Genet. 2005 Nov 5;139B(1):69-72
pubmed: 16152568
Methods Mol Biol. 2019;2049:419-444
pubmed: 31602625
Biochem J. 2000 Mar 15;346 Pt 3:857-64
pubmed: 10698717
Cell Metab. 2014 Jan 7;19(1):49-57
pubmed: 24411938
Nature. 2006 Aug 31;442(7106):1054-7
pubmed: 16929306
Genetics. 2012 Sep;192(1):73-105
pubmed: 22964838
Dis Model Mech. 2015 Jun;8(6):509-26
pubmed: 26035862
J Neuropathol Exp Neurol. 2011 Mar;70(3):167-76
pubmed: 21293295
Drug Metab Dispos. 2018 Jan;46(1):41-45
pubmed: 29109113
Drug Metab Pharmacokinet. 2015 Feb;30(1):3-20
pubmed: 25760527
Drug Metab Dispos. 2009 Apr;37(4):706-9
pubmed: 19171676
PLoS Biol. 2007 May;5(5):e97
pubmed: 17425406
Pharmacogenomics J. 2007 Apr;7(2):133-43
pubmed: 16801938
J Neurosci. 2020 Sep 9;40(37):7013-7026
pubmed: 32801157

Auteurs

Evan J Brettrager (EJ)

Department of Pharmacology and Toxicology, University of Alabama at Birmingham, 155 Volker Hall, 1720 2nd Ave S., Birmingham, AL, 35294-0019, USA.

Arthur W Meehan (AW)

Department of Pharmacology and Toxicology, University of Alabama at Birmingham, 155 Volker Hall, 1720 2nd Ave S., Birmingham, AL, 35294-0019, USA.

Charles N Falany (CN)

Department of Pharmacology and Toxicology, University of Alabama at Birmingham, 155 Volker Hall, 1720 2nd Ave S., Birmingham, AL, 35294-0019, USA.

Robert C A M van Waardenburg (RCAM)

Department of Pharmacology and Toxicology, University of Alabama at Birmingham, 155 Volker Hall, 1720 2nd Ave S., Birmingham, AL, 35294-0019, USA. rvanwaar@uab.edu.

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Classifications MeSH