GRX1 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: GRX1
Primary source: SGD:S000000540
Locus tag: YCL035C
See related: AllianceGenome:SGD:S000000540; FungiDB:YCL035C; VEuPathDB:YCL035C
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 glutathione peroxidase activity and glutathione transferase activity. Involved in cellular response to oxidative stress and protein glutathionylation. Located in cytoplasm and nucleus. Orthologous to several human genes including GLRX2 (glutaredoxin 2). [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

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Location:: chromosome: III

Exon count:: 1

Sequence:: Chromosome: III; NC_001135.5 (60841..61173, complement)

Chromosome III - NC_001135.5 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001135.5

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Molecular characterization of the Grx1 in complex with reduced glutathione has been reported.
Title: High-resolution crystal structure of the reduced Grx1 from Saccharomyces cerevisiae.
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.
Grx1p and Grx2p protect against Selenite-induced cell death.
Title: Selenite-induced cell death in Saccharomyces cerevisiae: protective role of glutaredoxins.
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.
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.
Comparative structural analyses of the oxidized and glutathionylated Grx1 illustrate the conformational changes of residues at different redox states, whose roles during catalysis are further compared with the homologous structures.
Title: Glutathionylation-triggered conformational changes of glutaredoxin Grx1 from the yeast Saccharomyces cerevisiae.
Redox-sensitive yellow fluorescent protein fused to glutaredoxin 1 (Grx1p). Intramolecular transfer of reducing equivalents made the fusion protein kinetically superior in reactions with glutathione.
Title: Mechanistic insight provided by glutaredoxin within a fusion to redox-sensitive yellow fluorescent protein.
Glutaredoxin Grx1p has been crystallized both as an independent protein and in a protein fusion with histidine-tagged yellow fluorescent protein.
Title: Crystallization of mutant forms of glutaredoxin Grx1p from yeast.

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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 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 protein glutathionylation	IGI Inferred from Genetic Interaction more info	PubMed

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

General protein information

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Preferred Names: dithiol glutaredoxin GRX1

NP_009895.1

EC 1.11.1.9

EC 2.5.1.18

Glutathione-dependent disulfide oxidoreductase; hydroperoxide and superoxide-radical responsive, heat-stable, with active site cysteine pair; protects cells from oxidative damage; GRX1 has a paralog, GRX2, that arose from the whole genome duplication; 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_001135.5 Reference assembly

Range

60841..61173 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001178680.1 → NP_009895.1 TPA: dithiol glutaredoxin GRX1 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_009895.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VQY0, P25373

UniProtKB/TrEMBL

A6ZTF5, B3LU47, C7GSZ2, C8Z454, G2W9Z0, N1P7Z5

Conserved Domains (1) summary

cd03419
Location:19 → 92

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, ...