TRX1 thioredoxin TRX1 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: TRX1
Official Full Name: thioredoxin TRX1
Primary source: SGD:S000004033
Locus tag: YLR043C
See related: AllianceGenome:SGD:S000004033; FungiDB:YLR043C; VEuPathDB:YLR043C
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as: LMA1
Summary: Enables disulfide oxidoreductase activity. Involved in several processes, including Golgi vesicle transport; cell redox homeostasis; and vacuole organization. Located in cytosol and mitochondrial intermembrane space. Orthologous to human TXN (thioredoxin). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See TRX1 in Genome Data Viewer

Location:: chromosome: XII

Exon count:: 1

Sequence:: Chromosome: XII; NC_001144.5 (231702..232013, complement)

Chromosome XII - NC_001144.5 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001144.5

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

These results revealed that the thioredoxin redox potential and redox charge closely tracked flux perturbations showing that these indices could be used as surrogate measures of the flux in vivo and, provide a mechanistic explanation for the previously observed correlations between thioredoxin oxidation and certain pathologies.
Title: The thioredoxin redox potential and redox charge are surrogate measures for flux in the thioredoxin system.
NMR spectroscopic studies of yeast TRX1 provide insights into the mechanism for the closing of the water cavity.
Title: Structures of the reduced and oxidized state of the mutant D24A of yeast thioredoxin 1: insights into the mechanism for the closing of the water cavity.
TRX1 is required to maintain the IMS small Tim proteins in reduced forms and facilitate their mitochondrial import
Title: Cytosolic thioredoxin system facilitates the import of mitochondrial small Tim proteins.
Results show that an oxidized sulfiredoxin under disulfide state is formed between the catalytic Cys(84) and Cys(48), and this oxidized is reduced selectively by thioredoxin.
Title: Catalytic mechanism of Sulfiredoxin from Saccharomyces cerevisiae passes through an oxidized disulfide sulfiredoxin intermediate that is reduced by thioredoxin.
Trx1 and Trx2 are essential for the nuclear accumulation of Msn2/4 and Maf1.
Title: H2O2 activates the nuclear localization of Msn2 and Maf1 through thioredoxins in Saccharomyces cerevisiae.
study solved the crystal structures of oxidized Trx1 and glutathionylated Trx1Cys33Ser mutant at 1.76 and 1.80 A, respectively; kinetic studies proved that Met35Arg mutation could alter the apparent K(m) and V(max) values of the reaction
Title: Structural and kinetic analysis of Saccharomyces cerevisiae thioredoxin Trx1: implications for the catalytic mechanism of GSSG reduced by the thioredoxin system.
X-ray diffraction analysis of glutathionylated Trx1 C33S mutant from yeast
Title: Purification, crystallization and preliminary X-ray diffraction analysis of glutathionylated Trx1 C33S mutant from yeast.
Human wt p53 expression in yeast leads to gene repression of thioredoxin (TRX1/2), a highly conserved multifunctional antioxidative and antiapoptotic protein family.
Title: Human p53 induces cell death and downregulates thioredoxin expression in Saccharomyces cerevisiae.
The cytosolic form of thioredoxin Trx1 has been cloned, expressed, purified and crystallized.
Title: Expression, purification, crystallization and preliminary X-ray diffraction analysis of thioredoxin Trx1 from 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 disulfide oxidoreductase activity	IDA Inferred from Direct Assay more info	PubMed
enables protein-disulfide reductase activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in cell redox homeostasis	IGI Inferred from Genetic Interaction more info	PubMed
involved_in deoxyribonucleotide biosynthetic process	IEA Inferred from Electronic Annotation more info
involved_in endoplasmic reticulum to Golgi vesicle-mediated transport	IDA Inferred from Direct Assay more info	PubMed
involved_in protein deglutathionylation	IDA Inferred from Direct Assay more info	PubMed
involved_in protein deglutathionylation	IGI Inferred from Genetic Interaction more info	PubMed
involved_in protein transport	IEA Inferred from Electronic Annotation more info
involved_in retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum	IDA Inferred from Direct Assay more info	PubMed
involved_in vacuole fusion, non-autophagic	IDA Inferred from Direct Assay more info	PubMed
involved_in vacuole inheritance	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in Golgi apparatus	IEA Inferred from Electronic Annotation more info
located_in Golgi membrane	IEA Inferred from Electronic Annotation more info
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
located_in cytosol	HDA more info	PubMed
located_in cytosol	IDA Inferred from Direct Assay more info	PubMed
located_in cytosol	IPI Inferred from Physical Interaction more info	PubMed
located_in membrane	IEA Inferred from Electronic Annotation more info
located_in mitochondrial intermembrane space	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrial intermembrane space	IEA Inferred from Electronic Annotation more info
located_in mitochondrion	HDA more info	PubMed
located_in mitochondrion	IEA Inferred from Electronic Annotation more info
located_in nucleus	HDA more info	PubMed
located_in nucleus	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: thioredoxin TRX1

NP_013144.1

Cytoplasmic thioredoxin isoenzyme; part of the thioredoxin system that protects cells from oxidative and reductive stress; subunit of the LMA1 complex, with Pbi2p, that promotes vacuole inheritance; cofactor for Tsa1p; required for ER-Golgi transport; facilitates mitochondrial import of small Tims (Tim9p, Tim10p, Tim13p) by maintaining them in reduced form along with Trx2p; component of a signal transduction redox relay in a light sensing pathway; abundance increases under DNA replication stress