ArticleProceedings of the National Academy of Sciences of the United States of America2013
Involvement of protein IF2 N domain in ribosomal subunit joining revealed from architecture and function of the full-length initiation factor.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers, 1 of them a synthesis that pooled it.
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Who cites it
40 citing papers in PubMed, 1 synthesis or guideline pooled it, 68 citations in OpenAlex.
- Repurposing drugs for treatment of tuberculosis: a role for non-steroidal anti-inflammatory drugs.British medical bulletin · 2016Pooled it
- Molecular mechanism of IF1- and IF2-driven translation initiation in bacteria.bioRxiv : the preprint server for biology · 2026Article
- A Microscale Platform for the Comprehensive Analysis of Bacterial Translation Initiation.International journal of molecular sciences · 2026Article
- Evolution of Translation Initiation Factor 2 Extensions Links Initiation to Bacterial Stress Response.bioRxiv : the preprint server for biology · 2026Article
- A complex between IF2 and NusA suggests early coupling of transcription-translation.Nature communications · 2025Article
- The origins and evolution of translation factors.Trends in genetics : TIG · 2025Review
- Bacterial IF2's N-terminal IDR drives cold-induced phase separation and promotes fitness during cold stress.bioRxiv : the preprint server for biology · 2025Article
- YfmR is a translation factor that prevents ribosome stalling and cell death in the absence of EF-P.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- YfmR is a translation factor that prevents ribosome stalling and cell death in the absence of EF-P.bioRxiv : the preprint server for biology · 2023Article
- Translation initiation of leaderless and polycistronic transcripts in mammalian mitochondria.Nucleic acids research · 2023Article
- Early divergence of translation initiation and elongation factors.Protein science : a publication of the Protein Society · 2022Article
- Analysis of lineage-specific protein family variability in prokaryotes combined with evolutionary reconstructions.Biology direct · 2022Article
- Role of aIF5B in archaeal translation initiation.Nucleic acids research · 2022Article
- Compact IF2 allows initiator tRNA accommodation into the P site and gates the ribosome to elongation.Nature communications · 2022Article
- Translation initiation site of mRNA is selected through dynamic interaction with the ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Zero-mode waveguides and nanopore-based sequencing technologies accelerate single-molecule studies.Biophysics and physicobiology · 2022Article
- Weakening the IF2-fMet-tRNA Interaction Suppresses the Lethal Phenotype Caused by GTPase Inactivation.International journal of molecular sciences · 2021Article
- Distinct pre-initiation steps in human mitochondrial translation.Nature communications · 2020Article
- Disparate Phenotypes Resulting from Mutations of a Single Histidine in Switch II ofInternational journal of molecular sciences · 2020Article
- Ribosome assembly defects subvert initiation Factor3 mediated scrutiny of bona fide start signal.Nucleic acids research · 2019Article
Corrections and comments
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Authors and funding
14 authors at 8 institutions in 5 countries.
Funding
Abstract
Translation initiation factor 2 (IF2) promotes 30S initiation complex (IC) formation and 50S subunit joining, which produces the 70S IC. The architecture of full-length IF2, determined by small angle X-ray diffraction and cryo electron microscopy, reveals a more extended conformation of IF2 in solution and on the ribosome than in the crystal. The N-terminal domain is only partially visible in the 30S IC, but in the 70S IC, it stabilizes interactions between IF2 and the L7/L12 stalk of the 50S, and on its deletion, proper N-formyl-methionyl(fMet)-tRNA(fMet) positioning and efficient transpeptidation are affected. Accordingly, fast kinetics and single-molecule fluorescence data indicate that the N terminus promotes 70S IC formation by stabilizing the productive sampling of the 50S subunit during 30S IC joining. Together, our data highlight the dynamics of IF2-dependent ribosomal subunit joining and the role played by the N terminus of IF2 in this process.
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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.