GRX2 dithiol glutaredoxin GRX2 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: GRX2
Official Full Name: dithiol glutaredoxin GRX2
Primary source: SGD:S000002921
Locus tag: YDR513W
See related: AllianceGenome:SGD:S000002921; FungiDB:YDR513W; VEuPathDB:YDR513W
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: TTR1
Summary: Enables disulfide oxidoreductase activity; glutathione peroxidase activity; and glutathione transferase activity. Involved in cellular response to oxidative stress and glutathione metabolic process. Located in cytosol and mitochondrion. Orthologous to human GLRX2 (glutaredoxin 2). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See GRX2 in Genome Data Viewer

Location:: chromosome: IV

Exon count:: 1

Sequence:: Chromosome: IV; NC_001136.10 (1471017..1471448)

Chromosome IV - NC_001136.10 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001136.10

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Deletion of either Grx1 or Grx2 shortened yeast CLS. Quantitative proteomics revealed that GRX deletion decreased the expression of stress-response proteins, leading to increased cellular reactive oxygen species accumulation and, subsequently, intracellular acidification. This activated the Ras/protein kinase A (PKA) signaling pathway.
Title: Glutaredoxin Deletion Shortens Chronological Life Span in Saccharomyces cerevisiae via ROS-Mediated Ras/PKA Activation.
Data show that the gatekeeper function of glutaredoxin Grx2 is dependent on its concentration in the mitochondrial intermembrane space (IMS).
Title: Kinetic control by limiting glutaredoxin amounts enables thiol oxidation in the reducing mitochondrial intermembrane space.
One target protein, Rib3p, which has as yet an undefined function in respiration, was confirmed to have its Cys56 reversibly S-glutathionylated in vitro in a Grx2p dependent process.
Title: Thiol redox proteomics identifies differential targets of cytosolic and mitochondrial glutaredoxin-2 isoforms in Saccharomyces cerevisiae. Reversible S-glutathionylation of DHBP synthase (RIB3).
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.
Grx1p and Grx2p protect against Selenite-induced cell death.
Title: Selenite-induced cell death in Saccharomyces cerevisiae: protective role of glutaredoxins.
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.
analysis of the structural basis for the different activities of yeast Grx1 and Grx2
Title: Structural basis for the different activities of yeast Grx1 and Grx2.
Mutations on key basic residues drastically affect the cellular fate of the protein, showing that evolutionary diversification of Grx2 structural and functional properties are strictly dependent on the sequence of the targeting signal peptide.
Title: Structure and function of yeast glutaredoxin 2 depend on postranslational processing and are related to subcellular distribution.
We hypothesize that the substitutions of Ser23 and Gln52 in yGrx1 by Ala23 and Glu52 in yGrx2 modify the capability of the active-site C-terminal cysteine to attack the mixed disulfide between the N-terminal active-site cysteine and glutathione molecule
Title: Structural aspects of the distinct biochemical properties of glutaredoxin 1 and glutaredoxin 2 from Saccharomyces cerevisiae.
glutaredoxin 2 and cytosolic thioredoxins have roles in cysteinyl-based redox modification of the 20S proteasome
Title: Role of glutaredoxin 2 and cytosolic thioredoxins in cysteinyl-based redox modification of the 20S proteasome.

Submit: New GeneRIF Correction See all GeneRIFs (12)

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	IMP Inferred from Mutant Phenotype more info	PubMed
enables glutathione disulfide oxidoreductase activity	IBA Inferred from Biological aspect of Ancestor more info
enables glutathione peroxidase activity	IDA Inferred from Direct Assay more info	PubMed
enables glutathione peroxidase activity	IEA Inferred from Electronic Annotation more info
enables glutathione transferase activity	IDA Inferred from Direct Assay more info	PubMed
enables glutathione transferase activity	IEA Inferred from Electronic Annotation more info
enables oxidoreductase activity	IEA Inferred from Electronic Annotation more info
enables transferase activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
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
involved_in cellular response to oxidative stress	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in glutathione metabolic process	IGI Inferred from Genetic Interaction more info	PubMed

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

General protein information

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Preferred Names: dithiol glutaredoxin GRX2

NP_010801.1

EC 1.11.1.9

EC 2.5.1.18

Cytoplasmic glutaredoxin; thioltransferase, glutathione-dependent disulfide oxidoreductase involved in maintaining redox state of target proteins, also exhibits glutathione peroxidase activity, expression induced in response to stress; GRX2 has two in-frame start codons resulting in a shorter isoform that is retained in the cytosol and a longer form translocated to the mitochondrial matrix; GRX2 has a paralog, GRX1, that arose from the whole genome duplication

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_001136.10 Reference assembly

Range

1471017..1471448

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001180821.1 → NP_010801.1 TPA: dithiol glutaredoxin GRX2 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_010801.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VTD4, P17695, Q6B234

UniProtKB/TrEMBL

A6ZZA0, B3LFF7, C7GKU6, G2WBP0

Conserved Domains (1) summary

cd03419
Location:53 → 137

GRX_GRXh_1_2_like; Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of proteins similar to human GRXs, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, ...