ArticleThe EMBO journal2011
Activation of initiation factor 2 by ligands and mutations for rapid docking of ribosomal subunits.
Article in The EMBO journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- A complex between IF2 and NusA suggests early coupling of transcription-translation.Nature communications · 2025Article
- The alarmones (p)ppGpp directly regulate translation initiation during entry into quiescence.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Roles of elusive translational GTPases come to light and inform on the process of ribosome biogenesis in bacteria.Molecular microbiology · 2018Review
- IF2 and unique features of initiator tRNARNA biology · 2018Article
- A conformational switch in initiation factor 2 controls the fidelity of translation initiation in bacteria.Nature communications · 2017Article
- Proofreading neutralizes potential error hotspots in genetic code translation by transfer RNAs.RNA (New York, N.Y.) · 2016Article
- Intersubunit Bridges of the Bacterial Ribosome.Journal of molecular biology · 2016Review
- Roles of helix H69 of 23S rRNA in translation initiation.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- The emerging role of rectified thermal fluctuations in initiator aa-tRNA- and start codon selection during translation initiation.Biochimie · 2015Review
- Ribosomal initiation complex-driven changes in the stability and dynamics of initiation factor 2 regulate the fidelity of translation initiation.Journal of molecular biology · 2015Article
- Structural insight into the recognition of amino-acylated initiator tRNA by eIF5B in the 80S initiation complex.BMC structural biology · 2014Article
- eIF5B employs a novel domain release mechanism to catalyze ribosomal subunit joining.The EMBO journal · 2014Article
- Structure of the protein core of translation initiation factor 2 in apo, GTP-bound and GDP-bound forms.Acta crystallographica. Section D, Biological crystallography · 2013Article
- Translation initiation without IF2-dependent GTP hydrolysis.Nucleic acids research · 2012Article
- Role of helix 44 of 16S rRNA in the fidelity of translation initiation.RNA (New York, N.Y.) · 2012Article
- GTPases IF2 and EF-G bind GDP and the SRL RNA in a mutually exclusive manner.Scientific reports · 2012Article
- Formyl-methionine as a degradation signal at the N-termini of bacterial proteins.Microbial cell (Graz, Austria)Article
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4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We previously identified mutations in the GTPase initiation factor 2 (IF2), located outside its tRNA-binding domain, compensating strongly (A-type) or weakly (B-type) for initiator tRNA formylation deficiency. We show here that rapid docking of 30S with 50S subunits in initiation of translation depends on switching 30S subunit-bound IF2 from its inactive to active form. Activation of wild-type IF2 requires GTP and formylated initiator tRNA (fMet-tRNA(i)). In contrast, extensive activation of A-type IF2 occurs with only GTP or with GDP and fMet-tRNA(i), implying a passive role for initiator tRNA as activator of IF2 in subunit docking. The theory of conditional switching of GTPases quantitatively accounts for all our experimental data. We find that GTP, GDP, fMet-tRNA(i) and A-type mutations multiplicatively increase the equilibrium ratio, K, between active and inactive forms of IF2 from a value of 4 × 10(-4) for wild-type apo-IF2 by factors of 300, 8, 80 and 20, respectively. Functional characterization of the A-type mutations provides keys to structural interpretation of conditional switching of IF2 and other multidomain GTPases.
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