GUS1 glutamate--tRNA ligase GUS1 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: GUS1
Official Full Name: glutamate--tRNA ligase GUS1
Primary source: SGD:S000003214
Locus tag: YGL245W
See related: AllianceGenome:SGD:S000003214; FungiDB:YGL245W; VEuPathDB:YGL245W
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: GSN1
Summary: Enables glutamate-tRNA ligase activity and sequence-specific mRNA binding activity. Involved in glutamyl-tRNA aminoacylation. Located in cytoplasmic stress granule and mitochondrion. Part of methionyl glutamyl tRNA synthetase complex. [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See GUS1 in Genome Data Viewer

Location:: chromosome: VII

Exon count:: 1

Sequence:: Chromosome: VII; NC_001139.9 (39023..41149)

Chromosome VII - NC_001139.9 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001139.9

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

the eukaryote-specific protein domains of GluRS and GlnRS substantially influence amino acid binding, tRNA binding and aminoacylation efficiency, but they play no role in either specific nucleotide readout or discrimination against noncognate tRNA
Title: Coevolution of specificity determinants in eukaryotic glutamyl- and glutaminyl-tRNA synthetases.
cytosolic glutamyl-tRNA synthetase ((c)ERS) is imported into mitochondria, where it constitutes the mitochondrial nondiscriminating ERS that generates the mitochondrial mischarged glutamyl-tRNA(Gln) substrate for the AdT
Title: Yeast mitochondrial Gln-tRNA(Gln) is generated by a GatFAB-mediated transamidation pathway involving Arc1p-controlled subcellular sorting of cytosolic GluRS.
assembly of the Arc1p-synthetase complex is mediated exclusively by the N-terminal domains of the synthetases and that the two enzymes bind to largely independent sites on Arc1p.
Title: Molecular determinants of the yeast Arc1p-aminoacyl-tRNA synthetase complex assembly.
These results are consistent with a model according to which Arc1p is a bifunctional protein involved in the subcellular localization of ScMetRS and ScGluRS via its N-terminal domain and of tRNA via its C-terminal domain.
Title: Arc1p is required for cytoplasmic confinement of synthetases and tRNA.
The structure of the interacting domain of yeast glutamyl-tRNA synthetase (GluRS) and its accessory protein Arc1p was determined and refined to 1.9 A resolution.
Title: Structures of the interacting domains from yeast glutamyl-tRNA synthetase and tRNA-aminoacylation and nuclear-export cofactor Arc1p reveal a novel function for an old fold.

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Pathways from PubChem

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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 ATP binding	IEA Inferred from Electronic Annotation more info
enables aminoacyl-tRNA ligase activity	IEA Inferred from Electronic Annotation more info
enables glutamate-tRNA ligase activity	IBA Inferred from Biological aspect of Ancestor more info
enables glutamate-tRNA ligase activity	IDA Inferred from Direct Assay more info	PubMed
enables glutamate-tRNA ligase activity	IEA Inferred from Electronic Annotation more info
enables mRNA binding	HDA more info	PubMed
enables sequence-specific mRNA binding	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in glutamyl-tRNA aminoacylation	IBA Inferred from Biological aspect of Ancestor more info
involved_in glutamyl-tRNA aminoacylation	IDA Inferred from Direct Assay more info	PubMed
involved_in glutamyl-tRNA aminoacylation	IEA Inferred from Electronic Annotation more info
involved_in translation	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
located_in cytoplasm	HDA more info	PubMed
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
located_in cytoplasmic stress granule	HDA more info	PubMed
located_in cytoplasmic stress granule	IDA Inferred from Direct Assay more info	PubMed
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
part_of methionyl glutamyl tRNA synthetase complex	IBA Inferred from Biological aspect of Ancestor more info
part_of methionyl glutamyl tRNA synthetase complex	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrion	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrion	IEA Inferred from Electronic Annotation more info
part_of protein-containing complex	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: glutamate--tRNA ligase GUS1

NP_011269.2

EC 6.1.1.17

Glutamyl-tRNA synthetase (GluRS); forms a complex with methionyl-tRNA synthetase (Mes1p) and Arc1p; complex formation increases the catalytic efficiency of both tRNA synthetases and ensures their correct localization to the cytoplasm; 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_001139.9 Reference assembly

Range

39023..41149

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001181111.1 → NP_011269.2 TPA: glutamate--tRNA ligase GUS1 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_011269.2

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VV90, P46655

UniProtKB/TrEMBL

A6ZTU6, B3LHT7, C7GNZ1, G2WDL5, N1P367

Conserved Domains (2) summary

TIGR00463
Location:102 → 696

gltX_arch; glutamyl-tRNA synthetase, archaeal and eukaryotic family

cl02776
Location:72 → 128

GST_C_family; C-terminal, alpha helical domain of the Glutathione S-transferase family