PRX1 thioredoxin peroxidase PRX1 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: PRX1
Official Full Name: thioredoxin peroxidase PRX1
Primary source: SGD:S000000160
Locus tag: YBL064C
See related: AllianceGenome:SGD:S000000160; FungiDB:YBL064C; VEuPathDB:YBL064C
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary: Enables thioredoxin peroxidase activity. Involved in cell redox homeostasis. Located in mitochondrion. Orthologous to human PRDX6 (peroxiredoxin 6). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See PRX1 in Genome Data Viewer

Location:: chromosome: II

Exon count:: 1

Sequence:: Chromosome: II; NC_001134.8 (100371..101156, complement)

Chromosome II - NC_001134.8 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001134.8

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Structural and biochemical analysis of 1-Cys peroxiredoxin ScPrx1 from Saccharomyces cerevisiae mitochondria.
Title: Structural and biochemical analysis of 1-Cys peroxiredoxin ScPrx1 from Saccharomyces cerevisiae mitochondria.
Study reveals that hyperoxidation of Prx1 serves as a switch-off mechanism to limit oxidation of matrix glutathione at high H2O2 concentrations.
Title: Hyperoxidation of mitochondrial peroxiredoxin limits H(2) O(2) -induced cell death in yeast.
Oct1 cleaved eight amino acid residues from the N-terminal region of Prx1 inside the matrix, without interfering with its peroxidase activity in vitro
Title: Proteolytic cleavage by the inner membrane peptidase (IMP) complex or Oct1 peptidase controls the localization of the yeast peroxiredoxin Prx1 to distinct mitochondrial compartments.
Prx1p is fairly well protected from overoxidation, questioning its role in a floodgate mechanism for H2O2 signaling
Title: Glutathione Is the Resolving Thiol for Thioredoxin Peroxidase Activity of 1-Cys Peroxiredoxin Without Being Consumed During the Catalytic Cycle.
these findings suggest that Srx1 regulates YPrx1 function and structure in yeast cells through a direct interaction.
Title: Reversal of 2-Cys peroxiredoxin oligomerization by sulfiredoxin.
Mitochondrial Prx1 functions as a redox signaling molecule that oxidizes Trx3 and promotes apoptosis.
Title: Oxidation of the yeast mitochondrial thioredoxin promotes cell death.
specific functions of two interacting redoxins: dually localized glutaredoxin 2 (Grx2p) and mitochondrial peroxiredoxin 1 (Prx1p)
Title: Biosynthetic and iron metabolism is regulated by thiol proteome changes dependent on glutaredoxin-2 and mitochondrial peroxiredoxin-1 in Saccharomyces cerevisiae.
Results suggest that although Trx is the reductant involved in the reduction of peroxides by 2-Cys-peroxiredoxin (Prx), glutaredoxin 2 might be the natural resolving partner of 1-Cys Prx through a monothiolic mechanism.
Title: Glutaredoxin participates in the reduction of peroxides by the mitochondrial 1-CYS peroxiredoxin in Saccharomyces cerevisiae.
The yeast mitochondrial 1-Cys Prx1 is reactivated by glutathionylation of the catalytic cysteine residue and subsequent reduction by thioredoxin reductase (Trr2) coupled with glutathione (GSH).
Title: Antioxidant activity of the yeast mitochondrial one-Cys peroxiredoxin is dependent on thioredoxin reductase and glutathione in vivo.
glucose repression effect is mediated by TOR1 and RAS2 through inhibition of MSN2/4
Title: Glucose repression of PRX1 expression is mediated by Tor1p and Ras2p through inhibition of Msn2/4p in Saccharomyces cerevisiae.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables peroxidase activity	IEA Inferred from Electronic Annotation more info
enables peroxiredoxin activity	IEA Inferred from Electronic Annotation more info
enables thioredoxin peroxidase activity	IBA Inferred from Biological aspect of Ancestor more info
enables thioredoxin peroxidase activity	IDA Inferred from Direct Assay more info	PubMed
enables thioredoxin peroxidase activity	IMP Inferred from Mutant Phenotype more info	PubMed

Process	Evidence Code	Pubs
involved_in cell redox homeostasis	IBA Inferred from Biological aspect of Ancestor more info
involved_in cell redox homeostasis	IDA Inferred from Direct Assay more info	PubMed
involved_in cell redox homeostasis	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in cellular oxidant detoxification	IEA Inferred from Electronic Annotation more info
involved_in cellular response to oxidative stress	IBA Inferred from Biological aspect of Ancestor more info

Component	Evidence Code	Pubs
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
located_in mitochondrion	HDA more info	PubMed
located_in mitochondrion	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrion	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: thioredoxin peroxidase PRX1

NP_009489.1

EC 1.11.1.25

EC 1.11.1.27

Mitochondrial peroxiredoxin with thioredoxin peroxidase activity; has a role in reduction of hydroperoxides; reactivation requires Trr2p and glutathione; induced during respiratory growth and oxidative stress; phosphorylated; protein abundance increases in response to DNA replication stress

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_001134.8 Reference assembly

Range

100371..101156 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001178304.1 → NP_009489.1 TPA: thioredoxin peroxidase PRX1 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_009489.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VPT6, P34227

UniProtKB/TrEMBL

A6ZKN5, B3LNJ9, B5VDS3, C7GNA2, C8Z3T2, G2W8U5, N1PAW7

Conserved Domains (1) summary

cd03016
Location:51 → 259

PRX_1cys; Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one conserved cysteine, which serves as the peroxidatic cysteine. They are homodimeric thiol-specific antioxidant (TSA) proteins that confer a protective role in cells by ...