ArticleProceedings of the National Academy of Sciences of the United States of America2003
Mapping the binding interface between human eukaryotic initiation factors 1A and 5B: a new interaction between old partners.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 91 citations in OpenAlex.
- Evolution of Translation Initiation Factor 2 Extensions Links Initiation to Bacterial Stress Response.bioRxiv : the preprint server for biology · 2026Article
- Synergistic Methods to Investigate Eukaryotic Translation and Its Quality Control.Journal of molecular biology · 2025Review
- Canonical translation factors eIF1A and eIF5B modulate the initiation step of repeat-associated non-AUG translation.Nucleic acids research · 2025Article
- Sex chromosome-encoded protein homologs: current progress and open questions.Nature structural & molecular biology · 2024Review
- Increased levels of eIF2A inhibit translation by sequestering 40S ribosomal subunits.Nucleic acids research · 2023Article
- Molecular architecture of 40S translation initiation complexes on the hepatitis C virus IRES.The EMBO journal · 2022Article
- Article
- Role of aIF5B in archaeal translation initiation.Nucleic acids research · 2022Article
- 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
- Recent Advances in Archaeal Translation Initiation.Frontiers in microbiology · 2020Review
- Eukaryotic Initiation Factor 5B (eIF5B) Cooperates with eIF1A and eIF5 to Facilitate uORF2-Mediated Repression of ATF4 Translation.International journal of molecular sciences · 2018Article
- Protein Synthesis Initiation in Eukaryotic Cells.Cold Spring Harbor perspectives in biology · 2018Review
- Human eIF5 and eIF1A Compete for Binding to eIF5B.Biochemistry · 2018Article
- Comparative sequence and structure analysis of eIF1A and eIF1AD.BMC structural biology · 2018Article
- Mutations in eIF5B Confer Thermosensitive and Pleiotropic Phenotypes via Translation Defects inThe Plant cell · 2017Article
- eIF1A/eIF5B interaction network and its functions in translation initiation complex assembly and remodeling.Nucleic acids research · 2016Article
- Initiation of mRNA translation in bacteria: structural and dynamic aspects.Cellular and molecular life sciences : CMLS · 2015Review
- Structural insight into the recognition of amino-acylated initiator tRNA by eIF5B in the 80S initiation complex.BMC structural biology · 2014Article
- Examining weak protein-protein interactions in start codon recognition via NMR spectroscopy.The FEBS journal · 2014Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The translation initiation factors (IFs) IF1/eIF1A and IF2e/IF5B have been conserved throughout all kingdoms. Although the central roles of the bacterial factors IF1 and IF2 were established long ago, the importance of their eukaryotic homologs, eukaryotic IFs (eIFs) eIF1A and eIF5B, has only recently become evident. The translation machinery in eukaryotes is more complex and accordingly, eIF1A and eIF5B seem to have acquired a number of new functions while also retaining many of the roles of bacterial IF1 and IF2. IF1 and IF2 have been shown to interact on the ribosome but no binding has been detected for the free factors. In contrast, yeast eIF1A and eIF5B have been reported to interact in the absence of ribosomes. Here, we have identified the binding interface between human eIF1A and the C-terminal domain of eIF5B by using solution NMR. That interaction interface involves the C termini of the two proteins, which are not present in bacterial IF1 and IF2. The interaction is, therefore, unique to eukaryotes. A structural model for the interaction of eIF1A and eIF5B in the context of the ribosome is presented. We propose that eIF1A and eIF5B simultaneously interact at two sites that are >50 A apart: through their C termini as reported here, and through an interface previously identified in bacterial IF1 and IF2. The binding between the C termini of eIF1A and eIF5B has implications for eukaryote-specific mechanisms of recruitment and release of translation IFs from the ribosome.
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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.