TIF5 translation initiation factor eIF5 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: TIF5
Official Full Name: translation initiation factor eIF5
Primary source: SGD:S000006245
Locus tag: YPR041W
See related: AllianceGenome:SGD:S000006245; FungiDB:YPR041W; VEuPathDB:YPR041W
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: SUI5
Summary: Enables GTPase regulator activity; translation initiation factor activity; and translation initiation factor binding activity. Involved in cytosolic ribosome assembly; formation of cytoplasmic translation initiation complex; and negative regulation of translational initiation. Part of eukaryotic 48S preinitiation complex and multi-eIF complex. Orthologous to human EIF5 (eukaryotic translation initiation factor 5). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See TIF5 in Genome Data Viewer

Location:: chromosome: XVI

Exon count:: 1

Sequence:: Chromosome: XVI; NC_001148.4 (648704..649921)

Chromosome XVI - NC_001148.4 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001148.4

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Substitutions of eIF5 residues involved in the eIF5-NTD/tRNAi interaction influenced initiation at near-cognate UUG codonsin vivo, and the closed/open PIC conformation in vitro, consistent with direct stabilization of the codon:anticodon duplex by the wild-type eIF5-NTD.
Title: Translational initiation factor eIF5 replaces eIF1 on the 40S ribosomal subunit to promote start-codon recognition.
These data uncover competition between eIF2B and eIF5 for eIF2-GTP/Met-tRNAi ternary complexes and identify that phosphorylated eIF2-GTP translation initiation intermediate complexes can be inhibited by eIF2B.
Title: Fail-safe control of translation initiation by dissociation of eIF2α phosphorylated ternary complexes.
eIF5-CTD (amino acids 241-405; Tif5p-B6) interacted with eIF1A (Tif11p).
Title: The interaction between eukaryotic initiation factor 1A and eIF5 retains eIF1 within scanning preinitiation complexes.
eIF2B has a second activity as a GDI displacement factor (GDF) that can recruit eIF2 from the eIF2*GDP/eIF5 GDI complex prior to GEF action.
Title: eIF2B promotes eIF5 dissociation from eIF2*GDP to facilitate guanine nucleotide exchange for translation initiation.
The direct interaction at eIF1 places eIF5 near the decoding site of the 40 S subunit.
Title: Eukaryotic initiation factor (eIF) 1 carries two distinct eIF5-binding faces important for multifactor assembly and AUG selection.
The eIF2/eIF5 complex represents a cytoplasmic reservoir for eIF2 that antagonizes eIF2B-promoted guanine nucleotide exchange, enabling coordinated regulation of translation initiation.
Title: An eIF5/eIF2 complex antagonizes guanine nucleotide exchange by eIF2B during translation initiation.
eIF-5 can form the multifactor complex with the ribosome 40S subunit.
Title: Reconfiguration of yeast 40S ribosomal subunit domains by the translation initiation multifactor complex.
eIF5 is critical for integrity of the scanning preinitiation complex and accurate control of GCN4 translation.
Title: Eukaryotic translation initiation factor 5 is critical for integrity of the scanning preinitiation complex and accurate control of GCN4 translation.
Data suggest strongly that the interaction between eIF5 and eIF1A is involved in maintaining the fidelity of start codon AUG recognition in vivo.
Title: Communication between eukaryotic translation initiation factors 5 and 1A within the ribosomal pre-initiation complex plays a role in start site selection.
Results describe the 1.5A crystal structure of eukaryotic initiation factor eIF5 C terminal domain, confirming that eIF5-CTD contains an atypical HEAT motif.
Title: Crystal structure of the C-terminal domain of S.cerevisiae eIF5.

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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 GDP-dissociation inhibitor activity	IBA Inferred from Biological aspect of Ancestor more info
enables GDP-dissociation inhibitor activity	IDA Inferred from Direct Assay more info	PubMed
enables GDP-dissociation inhibitor activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables GTP binding	IEA Inferred from Electronic Annotation more info
enables GTPase activator activity	IDA Inferred from Direct Assay more info	PubMed
enables GTPase activator activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables eukaryotic initiation factor eIF2 binding	IBA Inferred from Biological aspect of Ancestor more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables translation initiation factor activity	IBA Inferred from Biological aspect of Ancestor more info
enables translation initiation factor activity	IDA Inferred from Direct Assay more info	PubMed
enables translation initiation factor activity	IEA Inferred from Electronic Annotation more info
enables translation initiation factor binding	IDA Inferred from Direct Assay more info	PubMed
enables translation initiation factor binding	IPI Inferred from Physical Interaction more info	PubMed
enables zinc ion binding	RCA inferred from Reviewed Computational Analysis more info	PubMed

Process	Evidence Code	Pubs
involved_in cytosolic ribosome assembly	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in formation of cytoplasmic translation initiation complex	IBA Inferred from Biological aspect of Ancestor more info
involved_in formation of cytoplasmic translation initiation complex	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of translational initiation	IGI Inferred from Genetic Interaction more info	PubMed
involved_in negative regulation of translational initiation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in regulation of translational initiation	IDA Inferred from Direct Assay more info	PubMed
involved_in regulation of translational initiation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in translation	IEA Inferred from Electronic Annotation more info
involved_in translational initiation	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
part_of eukaryotic 48S preinitiation complex	IDA Inferred from Direct Assay more info	PubMed
part_of multi-eIF complex	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: translation initiation factor eIF5

NP_015366.1

Translation initiation factor eIF5; functions as both a GTPase-activating protein (GAP) that stimulates the hydrolysis of GTP bound to eIF-2, as part of the 43S preinitiation complex, and as a GDP dissociation inhibitor (GDI) to prevent recycling of eIF2; human ortholog eIF5 complements the yeast null mutant

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_001148.4 Reference assembly

Range

648704..649921

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001184138.1 → NP_015366.1 TPA: translation initiation factor eIF5 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_015366.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6W450, P38431

UniProtKB/TrEMBL

A6ZWT3, B3LLA1, C7GQ98, C8ZJ66, G2WPL8, N1P234

Conserved Domains (2) summary

cd11561
Location:242 → 392

W2_eIF5; C-terminal W2 domain of eukaryotic translation initiation factor 5

pfam01873
Location:8 → 127

eIF-5_eIF-2B; Domain found in IF2B/IF5