ArticleScientific reports2012
GTPases IF2 and EF-G bind GDP and the SRL RNA in a mutually exclusive manner.
Article in Scientific reports, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 11 citations in OpenAlex.
- EF-G Mutations Reveal Correlation between Power Stroke and Translocation Fidelity in Protein Synthesis.bioRxiv : the preprint server for biology · 2025Article
- Interaction of the GTPase Elongation Factor Like-1 with the Shwachman-Diamond Syndrome Protein and Its Missense Mutations.International journal of molecular sciences · 2018Article
- The ribosomal A-site finger is crucial for binding and activation of the stringent factor RelA.Nucleic acids research · 2018Article
- Phosphorylation of the Amyloid-Beta Peptide Inhibits Zinc-Dependent Aggregation, Prevents Na,K-ATPase Inhibition, and Reduces Cerebral Plaque Deposition.Frontiers in molecular neuroscience · 2018Article
- Reaction dynamics analysis of a reconstitutedProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Direct interaction of beta-amyloid with Na,K-ATPase as a putative regulator of the enzyme function.Scientific reports · 2016Article
- Initiation of mRNA translation in bacteria: structural and dynamic aspects.Cellular and molecular life sciences : CMLS · 2015Review
- Role of a ribosomal RNA phosphate oxygen during the EF-G-triggered GTP hydrolysis.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Translational GTPases (trGTPases) are involved in all four stages of protein biosynthesis: initiation, elongation, termination and ribosome recycling. The trGTPases Initiation Factor 2 (IF2) and Elongation Factor G (EF-G) respectively orchestrate initiation complex formation and translocation of the peptidyl-tRNA:mRNA complex through the bacterial ribosome. The ribosome regulates the GTPase cycle and efficiently discriminates between the GDP- and GTP-bound forms of these proteins. Using Isothermal Titration Calorimetry, we have investigated interactions of IF2 and EF-G with the sarcin-ricin loop of the 23S rRNA, a crucial element of the GTPase-associated center of the ribosome. We show that binding of IF2 and EF-G to a 27 nucleotide RNA fragment mimicking the sarcin-ricin loop is mutually exclusive with that of GDP, but not of GTP, providing a mechanism for destabilization of the ribosome-bound GDP forms of translational GTPases.
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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.