ArticleThe EMBO journal1999
Conserved bipartite motifs in yeast eIF5 and eIF2Bepsilon, GTPase-activating and GDP-GTP exchange factors in translation initiation, mediate binding to their common substrate eIF2.
Article in The EMBO journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 103 papers.
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Who cites it
103 citing papers in PubMed, 210 citations in OpenAlex.
- Molecular basis for the interactions of eIF2β with eIF5, eIF2B, and 5MP1 and their regulation by CK2.RNA (New York, N.Y.) · 2025Article
- Exploring the interaction dynamics of eukaryotic translation initiation factor 2.Biochemical Society transactions · 2025Review
- Translation Initiation Factor-2S2 (eIF2S2) Contributes to Cervical Carcinogenesis by Inhibiting the TGF-β/SMAD4 Signaling Pathway.Biomolecules & therapeutics · 2024Article
- eIF2β zinc-binding domain interacts with the eIF2γ subunit through the guanine nucleotide binding interface to promote Met-tRNAiMet binding.Bioscience reports · 2024Article
- Loss-of-function cancer-linked mutations in the EIF4G2 non-canonical translation initiation factor.Life science alliance · 2024Article
- The metaphorical swiss army knife: The multitude and diverse roles of HEAT domains in eukaryotic translation initiation.Nucleic acids research · 2022Review
- Dynamic interaction network involving the conserved intrinsically disordered regions in human eIF5.Biophysical chemistry · 2022Article
- Stepwise assembly of the eukaryotic translation initiation factor 2 complex.The Journal of biological chemistry · 2022Article
- Regulation of the interactions between human eIF5 and eIF1A by the CK2 kinase.Current research in structural biology · 2022Article
- The PCI domains are "winged" HEAT domains.PloS one · 2022Article
- Human oncoprotein 5MP suppresses general and repeat-associated non-AUG translation via eIF3 by a common mechanism.Cell reports · 2021Article
- Structural Differences in Translation Initiation between Pathogenic Trypanosomatids and Their Mammalian Hosts.Cell reports · 2020Article
- Endoplasmic reticulum stress: New insights into the pathogenesis and treatment of retinal degenerative diseases.Progress in retinal and eye research · 2020Review
- eIF2B and the Integrated Stress Response: A Structural and Mechanistic View.Biochemistry · 2020Article
- Structural basis for the inhibition of translation through eIF2α phosphorylation.Nature communications · 2019Article
- The structural basis of translational control by eIF2 phosphorylation.Nature communications · 2019Article
- Start Codon Recognition in Eukaryotic and Archaeal Translation Initiation: A Common Structural Core.International journal of molecular sciences · 2019Review
- Regulation of Hypoxia-Inducible Factor 1α during Hypoxia by DAP5-Induced Translation of PHD2.Molecular and cellular biology · 2018Article
- 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
- Fail-safe control of translation initiation by dissociation of eIF2α phosphorylated ternary complexes.eLife · 2017Article
43 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
5 authors at 1 institution in 2 countries.
Funding
Abstract
In the initiation phase of eukaryotic translation, eIF5 stimulates the hydrolysis of GTP bound to eIF2 in the 40S ribosomal pre-initiation complex, and the resultant GDP on eIF2 is replaced with GTP by the complex nucleotide exchange factor, eIF2B. Bipartite motifs rich in aromatic and acidic residues are conserved at the C-termini of eIF5 and the catalytic (epsilon) subunit of eIF2B. Here we show that these bipartite motifs are important for the binding of these factors, both in vitro and in vivo, to the beta subunit of their common substrate eIF2. We also find that three lysine-rich boxes in the N-terminal segment of eIF2beta mediate the binding of eIF2 to both eIF5 and eIF2B. Thus, eIF5 and eIF2Bepsilon employ the same sequence motif to facilitate interaction with the same segment of their common substrate. In agreement with this, archaea appear to lack eIF5, eIF2B and the lysine-rich binding domain for these factors in their eIF2beta homolog. The eIF5 bipartite motif is also important for its interaction with the eIF3 complex through the NIP1-encoded subunit of eIF3. Thus, the bipartite motif in eIF5 appears to be multifunctional, stimulating its recruitment to the 40S pre-initiation complex through interaction with eIF3 in addition to binding of its substrate eIF2.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.