ArticleRNA (New York, N.Y.)2001
Initiation factor IF 2 binds to the alpha-sarcin loop and helix 89 of Escherichia coli 23S ribosomal RNA.
Article in RNA (New York, N.Y.), 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
28 citing papers in PubMed, 73 citations in OpenAlex.
- A Novel Inhibitor of Translation Initiation Factor eIF5B inJournal of microbiology and biotechnology · 2024Article
- 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
- Chemical footprinting reveals conformational changes of 18S and 28S rRNAs at different steps of translation termination on the human ribosome.RNA (New York, N.Y.) · 2016Article
- Initiation of mRNA translation in bacteria: structural and dynamic aspects.Cellular and molecular life sciences : CMLS · 2015Review
- Discovery of novel mutations for clarithromycin resistance in Helicobacter pylori by using next-generation sequencing.The Journal of antimicrobial chemotherapy · 2014Article
- The SBP2 protein central to selenoprotein synthesis contacts the human ribosome at expansion segment 7L of the 28S rRNA.RNA (New York, N.Y.) · 2014Article
- The selenocysteine-specific elongation factor contains a novel and multi-functional domain.The Journal of biological chemistry · 2012Article
- Selenocysteine insertion sequence (SECIS)-binding protein 2 alters conformational dynamics of residues involved in tRNA accommodation in 80 S ribosomes.The Journal of biological chemistry · 2012Article
- GTPases IF2 and EF-G bind GDP and the SRL RNA in a mutually exclusive manner.Scientific reports · 2012Article
- Insertion domain within mammalian mitochondrial translation initiation factor 2 serves the role of eubacterial initiation factor 1.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Computational exploration of structural hypotheses for an additional sequence in a mammalian mitochondrial protein.PloS one · 2011Article
- GTP hydrolysis by IF2 guides progression of the ribosome into elongation.Molecular cell · 2009Article
- rRNA suppressor of a eukaryotic translation initiation factor 5B/initiation factor 2 mutant reveals a binding site for translational GTPases on the small ribosomal subunit.Molecular and cellular biology · 2009Article
- An unexpected type of ribosomes induced by kasugamycin: a look into ancestral times of protein synthesis?Molecular cell · 2009Article
- Function and ribosomal localization of aIF6, a translational regulator shared by archaea and eukarya.Nucleic acids research · 2009Article
- The sarcin-ricin loop of 23S rRNA is essential for assembly of the functional core of the 50S ribosomal subunit.RNA (New York, N.Y.) · 2008Article
- Multiple GTPases participate in the assembly of the large ribosomal subunit in Bacillus subtilis.Journal of bacteriology · 2006Article
- Initiation of protein synthesis in bacteria.Microbiology and molecular biology reviews : MMBR · 2005Review
- Testing the conservation of the translational machinery over evolution in diverse environments: assaying Thermus thermophilus ribosomes and initiation factors in a coupled transcription-translation system from Escherichia coli.Nucleic acids research · 2004Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
During initiation of protein synthesis in bacteria, translation initiation factor IF2 is responsible for the recognition of the initiator tRNA (fMet-tRNA). To perform this function, IF2 binds to the ribosome interacting with both 30S and 50S ribosomal subunits. Here we report the topographical localization of translation initiation factor IF2 on the 70S ribosome determined by base-specific chemical probing. Our results indicate that IF2 specifically protects from chemical modification two sites in domain V of 23S rRNA, namely A2476 and A2478, and residues around position 2660 in domain VI, the so-called sarcin-ricin loop. These footprints are generated by IF2 regardless of the presence of fMet-tRNA, GTP, mRNA, and IF1. IF2 causes no specific protection of 16S rRNA. We observe a decreased reactivity of residues A1418 and A1483, which is an indication that the initiation factor has a tightening effect on the association of ribosomal subunits. This result, confirmed by sucrose density gradient analysis, seems to be a universally conserved property of IF2.
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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.