ArticleNucleic acids research2016
eIF1A/eIF5B interaction network and its functions in translation initiation complex assembly and remodeling.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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27 citing papers in PubMed, 43 citations in OpenAlex.
- Evolution of Translation Initiation Factor 2 Extensions Links Initiation to Bacterial Stress Response.bioRxiv : the preprint server for biology · 2026Article
- The origins and evolution of translation factors.Trends in genetics : TIG · 2025Review
- Sex chromosome-encoded protein homologs: current progress and open questions.Nature structural & molecular biology · 2024Review
- CriticalNAR genomics and bioinformatics · 2024Article
- Start codon-associated ribosomal frameshifting mediates nutrient stress adaptation.Nature structural & molecular biology · 2023Article
- Review
- Translation regulatory factor BZW1 regulates preimplantation embryo development and compaction by restricting global non-AUG Initiation.Nature communications · 2022Article
- Molecular architecture of 40S translation initiation complexes on the hepatitis C virus IRES.The EMBO journal · 2022Article
- Article
- Dynamic interaction network involving the conserved intrinsically disordered regions in human eIF5.Biophysical chemistry · 2022Article
- Regulation of the interactions between human eIF5 and eIF1A by the CK2 kinase.Current research in structural biology · 2022Article
- Erosion of human X chromosome inactivation causes major remodeling of the iPSC proteome.Cell reports · 2021Article
- Established and Emerging Regulatory Roles of Eukaryotic Translation Initiation Factor 5B (eIF5B).Frontiers in genetics · 2021Review
- Impact of Eukaryotic Translation Initiation Factors on Breast Cancer: Still Much to Investigate.Cancers · 2020Review
- Control of Translation at the Initiation Phase During Glucose Starvation in Yeast.International journal of molecular sciences · 2019Review
- Protein Synthesis Initiation in Eukaryotic Cells.Cold Spring Harbor perspectives in biology · 2018Review
- Human eIF5 and eIF1A Compete for Binding to eIF5B.Biochemistry · 2018Article
- Article
- Comparative sequence and structure analysis of eIF1A and eIF1AD.BMC structural biology · 2018Article
- The Jigsaw Puzzle of mRNA Translation Initiation in Eukaryotes: A Decade of Structures Unraveling the Mechanics of the Process.Annual review of biophysics · 2018Article
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7 authors at 3 institutions in 1 country.
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Abstract
Eukaryotic translation initiation is a highly regulated process involving multiple steps, from 43S pre-initiation complex (PIC) assembly, to ribosomal subunit joining. Subunit joining is controlled by the G-protein eukaryotic translation initiation factor 5B (eIF5B). Another protein, eIF1A, is involved in virtually all steps, including subunit joining. The intrinsically disordered eIF1A C-terminal tail (eIF1A-CTT) binds to eIF5B Domain-4 (eIF5B-D4). The ribosomal complex undergoes conformational rearrangements at every step of translation initiation; however, the underlying molecular mechanisms are poorly understood. Here we report three novel interactions involving eIF5B and eIF1A: (i) a second binding interface between eIF5B and eIF1A; (ii) a dynamic intramolecular interaction in eIF1A between the folded domain and eIF1A-CTT; and (iii) an intramolecular interaction between eIF5B-D3 and -D4. The intramolecular interactions within eIF1A and eIF5B interfere with one or both eIF5B/eIF1A contact interfaces, but are disrupted on the ribosome at different stages of translation initiation. Therefore, our results indicate that the interactions between eIF1A and eIF5B are being continuously rearranged during translation initiation. We present a model how the dynamic eIF1A/eIF5B interaction network can promote remodeling of the translation initiation complexes, and the roles in the process played by intrinsically disordered protein segments.
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