TIF1 translation initiation factor eIF4A [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: TIF1
Official Full Name: translation initiation factor eIF4A
Primary source: SGD:S000001767
Locus tag: YKR059W
See related: AllianceGenome:SGD:S000001767; FungiDB:YKR059W; VEuPathDB:YKR059W
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 translation initiation factor activity. Involved in translational initiation. Is active in cytoplasm. Human ortholog(s) of this gene implicated in neurodevelopmental disorder with hypotonia and speech delay. Orthologous to human EIF4A1 (eukaryotic translation initiation factor 4A1) and EIF4A2 (eukaryotic translation initiation factor 4A2). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See TIF1 in Genome Data Viewer

Location:: chromosome: XI

Exon count:: 1

Sequence:: Chromosome: XI; NC_001143.9 (554987..556174)

Chromosome XI - NC_001143.9 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001143.9

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

eIF4G is retained on ribosomes elongating and terminating on short upstream ORFs to control reinitiation in yeast.
Title: eIF4G is retained on ribosomes elongating and terminating on short upstream ORFs to control reinitiation in yeast.
Distinct interactions of eIF4A and eIF4E with RNA helicase Ded1 stimulate translation in vivo.
Title: Distinct interactions of eIF4A and eIF4E with RNA helicase Ded1 stimulate translation in vivo.
RNA substrates affect eIF4A activities by modulating the kinetic partitioning of eIF4A between futile, unproductive, and productive cycles
Title: Single-stranded regions modulate conformational dynamics and ATPase activity of eIF4A to optimize 5'-UTR unwinding.
The results from this study identify protein complexes and pathways that will make ideal targets for combination therapies with eIF4A inhibitors.
Title: Characterisation of the biological response of Saccharomyces cerevisiae to the loss of an allele of the eukaryotic initiation factor 4A.
These findings reveal an eIF4A-independent role for eIF4B in addition to its function as eIF4A cofactor in promoting PIC attachment or scanning on structured mRNAs.
Title: eIF4B stimulates translation of long mRNAs with structured 5' UTRs and low closed-loop potential but weak dependence on eIF4G.
These results reveal and characterize an unexpected interdependence between the two RNA helicases and eIF4G, and suggest that Ded1p is an integral part of eIF4F, the complex comprising eIF4G, eIF4A, and eIF4E.
Title: Coupling between the DEAD-box RNA helicases Ded1p and eIF4A.
Findings suggest that Ded1 is critically required to promote scanning through secondary structures within 5' UTRs, and while eIF4A cooperates with Ded1 in this function, it also promotes a step of initiation common to virtually all yeast mRNAs.
Title: Genome-wide analysis of translational efficiency reveals distinct but overlapping functions of yeast DEAD-box RNA helicases Ded1 and eIF4A.
Yeast eIF4B strongly promotes productive interaction of eIF4A with the 43S*mRNA pre-initiation complex (PIC) in a manner required for efficient mRNA recruitment.
Title: Yeast eIF4B binds to the head of the 40S ribosomal subunit and promotes mRNA recruitment through its N-terminal and internal repeat domains.
Glucose depletion inhibits translation initiation via eukaryotic initiation factor 4a loss and subsequent 48S preinitiation complex accumulation
Title: Glucose depletion inhibits translation initiation via eIF4A loss and subsequent 48S preinitiation complex accumulation, while the pentose phosphate pathway is coordinately up-regulated.
structure of the complex formed by yeast eIF4G's middle domain and full-length eIF4A at 2.6-A resolution
Title: Crystal structure of the yeast eIF4A-eIF4G complex: an RNA-helicase controlled by protein-protein interactions.

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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 ATP hydrolysis activity	IEA Inferred from Electronic Annotation more info
enables ATP-dependent H2AZ histone chaperone activity	IEA Inferred from Electronic Annotation more info
enables ATP-dependent H3-H4 histone complex chaperone activity	IEA Inferred from Electronic Annotation more info
enables DNA clamp loader activity	IEA Inferred from Electronic Annotation more info
enables RNA binding	IEA Inferred from Electronic Annotation more info
enables RNA helicase activity	IEA Inferred from Electronic Annotation more info
enables chromatin extrusion motor activity	IEA Inferred from Electronic Annotation more info
enables cohesin loader activity	IEA Inferred from Electronic Annotation more info
enables helicase activity	IEA Inferred from Electronic Annotation more info
enables hydrolase activity	IEA Inferred from Electronic Annotation more info
enables nucleic acid binding	IEA Inferred from Electronic Annotation more info
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

Process	Evidence Code	Pubs
involved_in chromatin looping	IEA Inferred from Electronic Annotation more info
involved_in chromatin remodeling	IEA Inferred from Electronic Annotation more info
involved_in cytoplasmic translational initiation	IBA Inferred from Biological aspect of Ancestor more info
involved_in translation	IEA Inferred from Electronic Annotation more info
involved_in translational initiation	IDA Inferred from Direct Assay more info	PubMed
involved_in translational initiation	IEA Inferred from Electronic Annotation more info

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

General protein information

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Preferred Names: translation initiation factor eIF4A

NP_012985.3

Translation initiation factor eIF4A; DEAD-box RNA helicase that couples ATPase activity to mRNA binding and unwinding; ATP hydrolysis accelerates the recruitment of mRNA during 48S preinitiation complex (PIC) assembly; ATPase activity stimulated by either eIF4G1 or by the PIC in an eIF3g and eIFGi subunit-dependent manner, independent of eIF4E and eIF4G; subunit of the mRNA cap-binding protein complex (eIF4F) with eIF4E and eIF4G; 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_001143.9 Reference assembly

Range

554987..556174

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001179849.3 → NP_012985.3 TPA: translation initiation factor eIF4A [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_012985.3

Status: REVIEWED

UniProtKB/Swiss-Prot

A6ZQJ1, D6VW46, P10081

UniProtKB/TrEMBL

B3LRD4, C8ZCM2, G2WI87, N1P0H0, N1P0I8

Conserved Domains (1) summary

PTZ00424
Location:10 → 394

PTZ00424; helicase 45; Provisional