ArticleMolecular and cellular biology2000
Mutational analysis of mammalian translation initiation factor 5 (eIF5): role of interaction between the beta subunit of eIF2 and eIF5 in eIF5 function in vitro and in vivo.
Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 59 citations in OpenAlex.
- Integrative analysis of single-cell and bulk RNA sequencing data for discovery of senescent TAMs prognostic characteristics in neuroblastoma.BMC cancer · 2026Article
- Molecular basis for the interactions of eIF2β with eIF5, eIF2B, and 5MP1 and their regulation by CK2.RNA (New York, N.Y.) · 2025Article
- Structural basis for translational control by the human 48S initiation complex.Nature structural & molecular biology · 2025Article
- Na,K-ATPase as a target for endogenous cardiotonic steroids: What's the evidence?Genes & diseases · 2021Review
- Structural Differences in Translation Initiation between Pathogenic Trypanosomatids and Their Mammalian Hosts.Cell reports · 2020Article
- Deletion of eIF2β lysine stretches creates a dominant negative that affects the translation and proliferation in human cell line: A tool for arresting the cell growth.Cancer biology & therapy · 2017Article
- Na⁺Molecules (Basel, Switzerland) · 2017Review
- Time- and dose dependent actions of cardiotonic steroids on transcriptome and intracellular content of NaScientific reports · 2017Article
- Role of Eukaryotic Initiation Factors during Cellular Stress and Cancer Progression.Journal of nucleic acids · 2016Review
- Identification of Plasmodium falciparum Translation Initiation eIF2β Subunit: Direct Interaction with Protein Phosphatase Type 1.Frontiers in microbiology · 2016Article
- The interaction between eukaryotic initiation factor 1A and eIF5 retains eIF1 within scanning preinitiation complexes.Biochemistry · 2013Article
- Maternal separation with early weaning: a rodent model providing novel insights into neglect associated developmental deficits.Development and psychopathology · 2012Article
- 'Ribozoomin'--translation initiation from the perspective of the ribosome-bound eukaryotic initiation factors (eIFs).Current protein & peptide science · 2012Review
- Mechanisms of translational regulation by a human eIF5-mimic protein.Nucleic acids research · 2011Article
- Molecular mechanism of scanning and start codon selection in eukaryotes.Microbiology and molecular biology reviews : MMBR · 2011Review
- Assessing the components of the eIF3 complex and their phosphorylation status.Journal of proteome research · 2011Article
- Molecular view of 43 S complex formation and start site selection in eukaryotic translation initiation.The Journal of biological chemistry · 2010Review
- Crystal structure of the C-terminal domain of the ɛ subunit of human translation initiation factor eIF2B.Protein & cell · 2010Article
- Phosphorylation of plant translation initiation factors by CK2 enhances the in vitro interaction of multifactor complex components.The Journal of biological chemistry · 2009Article
- Structure of an archaeal heterotrimeric initiation factor 2 reveals a nucleotide state between the GTP and the GDP states.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Eukaryotic translation initiation factor 5 (eIF5) interacts with the 40S initiation complex (40S-eIF3-AUG-Met-tRNA(f)-eIF2-GTP) to promote the hydrolysis of ribosome-bound GTP. eIF5 also forms a complex with eIF2 by interacting with the beta subunit of eIF2. In this work, we have used a mutational approach to investigate the importance of eIF5-eIF2beta interaction in eIF5 function. Binding analyses with recombinant rat eIF5 deletion mutants identified the C terminus of eIF5 as the eIF2beta-binding region. Alanine substitution mutagenesis at sites within this region defined several conserved glutamic acid residues in a bipartite motif as critical for eIF5 function. The E346A,E347A and E384A,E385A double-point mutations each caused a severe defect in the binding of eIF5 to eIF2beta but not to eIF3-Nip1p, while a eIF5 hexamutant (E345A,E346A, E347A,E384A,E385A,E386A) showed negligible binding to eIF2beta. These mutants were also severely defective in eIF5-dependent GTP hydrolysis, in 80S initiation complex formation, and in the ability to stimulate translation of mRNAs in an eIF5-dependent yeast cell-free translation system. Furthermore, unlike wild-type rat eIF5, which can functionally substitute for yeast eIF5 in complementing in vivo a genetic disruption of the chromosomal copy of the TIF5 gene, the eIF5 double-point mutants allowed only slow growth of this DeltaTIF5 yeast strain, while the eIF5 hexamutant was unable to support cell growth and viability of this strain. These findings suggest that eIF5-eIF2beta interaction plays an essential role in eIF5 function in eukaryotic cells.
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