ArticleThe EMBO journal2014
eIF5B employs a novel domain release mechanism to catalyze ribosomal subunit joining.
Article in The EMBO journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 56 citations in OpenAlex.
- Overcoming Barriers to Clinical Translation: MG1 Maraba Virus as an Emerging Platform for Oncolytic Immunotherapy.Viruses · 2026Review
- Structural basis for translational control by the human 48S initiation complex.Nature structural & molecular biology · 2025Article
- C9orf72-linked arginine-rich dipeptide repeats aggravate pathological phase separation of G3BP1.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The intrinsically disordered region of eIF5B stimulates IRES usage and nucleates biological granule formation.Cell reports · 2023Article
- Early divergence of translation initiation and elongation factors.Protein science : a publication of the Protein Society · 2022Article
- Genome-Wide Identification and Expression Analysis of eIF Family Genes fromPlants (Basel, Switzerland) · 2022Article
- 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
- Article
- Established and Emerging Regulatory Roles of Eukaryotic Translation Initiation Factor 5B (eIF5B).Frontiers in genetics · 2021Review
- Structural basis for the transition from translation initiation to elongation by an 80S-eIF5B complex.Nature communications · 2020Article
- Long-range interdomain communications in eIF5B regulate GTP hydrolysis and translation initiation.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Recent Advances in Archaeal Translation Initiation.Frontiers in microbiology · 2020Review
- Article
- Characterizing Cellular Responses During Oncolytic Maraba Virus Infection.International journal of molecular sciences · 2019Article
- Protein Synthesis Initiation in Eukaryotic Cells.Cold Spring Harbor perspectives in biology · 2018Review
- The Interaction between the Ribosomal Stalk Proteins and Translation Initiation Factor 5B Promotes Translation Initiation.Molecular and cellular biology · 2018Article
- Identification of two novel host proteins interacting with Toxoplasma gondii 14-3-3 protein by yeast two-hybrid system.Parasitology research · 2018Article
- More than just scanning: the importance of cap-independent mRNA translation initiation for cellular stress response and cancer.Cellular and molecular life sciences : CMLS · 2017Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
eIF5B is a eukaryal translational GTPase that catalyzes ribosomal subunit joining to form elongation-competent ribosomes. Despite its central role in protein synthesis, the mechanistic details that govern the function of eIF5B or its archaeal and bacterial (IF2) orthologs remained unclear. Here, we present six high-resolution crystal structures of eIF5B in its apo, GDP- and GTP-bound form that, together with an analysis of the thermodynamics of nucleotide binding, provide a detailed picture of the entire nucleotide cycle performed by eIF5B. Our data show that GTP binding induces significant conformational changes in the two conserved switch regions of the G domain, resulting in the reorganization of the GTPase center. These rearrangements are accompanied by the rotation of domain II relative to the G domain and release of domain III from its stable contacts with switch 2, causing an increased intrinsic flexibility in the free GTP-bound eIF5B. Based on these data, we propose a novel domain release mechanism for eIF5B/IF2 activation that explains how eIF5B and IF2 fulfill their catalytic role during ribosomal subunit joining.
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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.