ArticleNucleic acids research2012
Translation initiation without IF2-dependent GTP hydrolysis.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 17 citations in OpenAlex.
- Weakening the IF2-fMet-tRNA Interaction Suppresses the Lethal Phenotype Caused by GTPase Inactivation.International journal of molecular sciences · 2021Article
- Disparate Phenotypes Resulting from Mutations of a Single Histidine in Switch II ofInternational journal of molecular sciences · 2020Article
- The Ribosome as a Switchboard for Bacterial Stress Response.Frontiers in microbiology · 2020Review
- How the initiating ribosome copes with ppGpp to translate mRNAs.PLoS biology · 2020Article
- Translation initiation factor IF2 contributes to ribosome assembly and maturation during cold adaptation.Nucleic acids research · 2019Article
- A model for the interaction of the G3-subdomain of Geobacillus stearothermophilus IF2 with the 30S ribosomal subunit.Protein science : a publication of the Protein Society · 2016Article
- Directional transition from initiation to elongation in bacterial translation.Nucleic acids research · 2015Article
- Initiation of mRNA translation in bacteria: structural and dynamic aspects.Cellular and molecular life sciences : CMLS · 2015Review
- eIF5B employs a novel domain release mechanism to catalyze ribosomal subunit joining.The EMBO journal · 2014Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Translation initiation factor IF2 is a guanine nucleotide-binding protein. The free energy change associated with guanosine triphosphate hydrolase (GTPase) activity of these proteins is believed to be the driving force allowing them to perform their functions as molecular switches. We examined role and relevance of IF2 GTPase and demonstrate that an Escherichia coli IF2 mutant bearing a single amino acid substitution (E571K) in its 30S binding domain (IF2-G3) can perform in vitro all individual translation initiation functions of wild type (wt) IF2 and supports faithful messenger RNA translation, despite having a reduced affinity for the 30S subunit and being completely inactive in GTP hydrolysis. Furthermore, the corresponding GTPase-null mutant of Bacillus stearothermophilus (E424K) can replace in vivo wt IF2 allowing an E. coli infB null mutant to grow with almost wt duplication times. Following the E571K (and E424K) mutation, which likely disrupts hydrogen bonding between subdomains G2 and G3, IF2 acquires a guanosine diphosphate (GDP)-like conformation, no longer responsive to GTP binding thereby highlighting the importance of interdomain communication in IF2. Our data underlie the importance of GTP as an IF2 ligand in the early initiation steps and the dispensability of the free energy generated by the IF2 GTPase in the late events of the translation initiation pathway.
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Registered trials
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.