Translation initiation factor 5A and its hypusine modification are essential for cell viability in the yeast Saccharomyces cerevisiae.

doi:10.1128/mcb.11.6.3105-3114.1991

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Article

Translation initiation factor 5A and its hypusine modification are essential for cell viability in the yeast Saccharomyces cerevisiae.

Molecular and cellular biology - 1 Jun 1991

Schnier J, Schwelberger H G, Smit-McBride Z, Kang H A, Hershey J W

Abstract excerpt

Translation intitiation factor eIF-5A (previously named eIF-4D) is a highly conserved protein that promotes formation of the first peptide bond. One of its lysine residues is modified by spermidine to form hypusine, a posttranslational modification unique to eIF-5A. To elucidate the function of e...

Topics

Amino Acid Sequence
Base Sequence
Blotting, Northern
Cloning, Molecular
Codon
Genes, Fungal
Genetic Vectors
Humans
Kinetics
Lysine
Mitochondria
Molecular Sequence Data

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Oligonucleotide Probes

Peptide Initiation Factors

Phenotype

Plasmids

Protein Processing, Post-Translational

RNA, Messenger

Source

Open in PubMed Open full text

Identifiers

PMID: 1903841
DOI: 10.1128/mcb.11.6.3105-3114.1991
PMCID: PMC360154

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-1903841-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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Translation initiation factor 5A and its hypusine modification are essential for cell viability in the yeast Saccharomyces cerevisiae.PMID 1903841Read ↗

Translation initiation factor eIF-5A expressed from either of two yeast genes or from human cDNA. Functional identity under aerobic and anaerobic conditions.Semantic proximity Read ↗

Structural modeling and mutational analysis of yeast eukaryotic translation initiation factor 5A reveal new critical residues and reinforce its involvement in protein synthesis.Semantic proximity Read ↗

Hypusine-containing protein eIF5A promotes translation elongation.Semantic proximity Read ↗

Characterization of yeast translation initiation factor 1A and cloning of its essential gene.Semantic proximity Read ↗

eIF5A is an indispensable protein for eukaryotic cellsSemantic proximity Read ↗

Rapid depletion of mutant eukaryotic initiation factor 5A at restrictive temperature reveals connections to actin cytoskeleton and cell cycle progression.Semantic proximity Read ↗

eIF5A is an indispensable protein for eukaryotic cellsSemantic proximity Read ↗

Genetic interactions of yeast eukaryotic translation initiation factor 5A (eIF5A) reveal connections to poly(A)-binding protein and protein kinase C signaling.Semantic proximity Read ↗

Temperature-sensitive eIF5A mutant accumulates transcripts targeted to the nonsense-mediated decay pathway.Semantic proximity Read ↗

Mutational analyses of human eIF5A-1--identification of amino acid residues critical for eIF5A activity and hypusine modification.Semantic proximity Read ↗

Characterization of translation initiation factor 5 (eIF5) from Saccharomyces cerevisiae. Functional homology with mammalian eIF5 and the effect of depletion of eIF5 on protein synthesis in vivo and in vitro.Semantic proximity Read ↗

Tandem affinity purification revealed the hypusine-dependent binding of eukaryotic initiation factor 5A to the translating 80S ribosomal complex.Semantic proximity Read ↗

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