ArticleNucleic acids research2007
L11 domain rearrangement upon binding to RNA and thiostrepton studied by NMR spectroscopy.
Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 55 citations in OpenAlex.
- Article
- Mechanism of Action of Ribosomally Synthesized and Post-Translationally Modified Peptides.Chemical reviews · 2022Review
- Glycogen synthase kinase-3β inhibits tubular regeneration in acute kidney injury by a FoxM1-dependent mechanism.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020Article
- Ribosomal Protein L11 Selectively Stabilizes a Tertiary Structure of the GTPase Center rRNA Domain.Journal of molecular biology · 2020Article
- YcaO-Dependent Posttranslational Amide Activation: Biosynthesis, Structure, and Function.Chemical reviews · 2017Review
- Thiostrepton interacts covalently with Rpt subunits of the 19S proteasome and proteasome substrates.Journal of cellular and molecular medicine · 2015Article
- Crystallographic analysis of archaeal ribosomal protein L11.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Substrate recognition and modification by the nosiheptide resistance methyltransferase.PloS one · 2015Article
- Structural basis and dynamics of multidrug recognition in a minimal bacterial multidrug resistance system.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Structure-activity relationships of thiostrepton derivatives: implications for rational drug design.Journal of computer-aided molecular design · 2014Article
- Principal component and clustering analysis on molecular dynamics data of the ribosomal L11·23S subdomain.Journal of molecular modeling · 2013Article
- Common chaperone activity in the G-domain of trGTPase protects L11-L12 interaction on the ribosome.Nucleic acids research · 2012Article
- A conserved proline switch on the ribosome facilitates the recruitment and binding of trGTPases.Nature structural & molecular biology · 2012Article
- Thiostrepton inhibits stable 70S ribosome binding and ribosome-dependent GTPase activation of elongation factor G and elongation factor 4.Nucleic acids research · 2012Article
- Thiostrepton and derivatives exhibit antimalarial and gametocytocidal activity by dually targeting parasite proteasome and apicoplast.Antimicrobial agents and chemotherapy · 2011Article
- Proteasome inhibitory activity of thiazole antibiotics.Cancer biology & therapy · 2011Article
- Identification of distinct thiopeptide-antibiotic precursor lead compounds using translation machinery assays.Chemistry & biology · 2009Article
- RNA in motion.Current opinion in chemical biology · 2008Review
- Multiple-site trimethylation of ribosomal protein L11 by the PrmA methyltransferase.Structure (London, England : 1993) · 2008Article
- Developmentally regulated cleavage of tRNAs in the bacterium Streptomyces coelicolor.Nucleic acids research · 2008Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ribosomal proteins are assumed to stabilize specific RNA structures and promote compact folding of the large rRNA. The conformational dynamics of the protein between the bound and unbound state play an important role in the binding process. We have studied those dynamical changes in detail for the highly conserved complex between the ribosomal protein L11 and the GTPase region of 23S rRNA. The RNA domain is compactly folded into a well defined tertiary structure, which is further stabilized by the association with the C-terminal domain of the L11 protein (L11(ctd)). In addition, the N-terminal domain of L11 (L11(ntd)) is implicated in the binding of the natural thiazole antibiotic thiostrepton, which disrupts the elongation factor function. We have studied the conformation of the ribosomal protein and its dynamics by NMR in the unbound state, the RNA bound state and in the ternary complex with the RNA and thiostrepton. Our data reveal a rearrangement of the L11(ntd), placing it closer to the RNA after binding of thiostrepton, which may prevent binding of elongation factors. We propose a model for the ternary L11-RNA-thiostrepton complex that is additionally based on interaction data and conformational information of the L11 protein. The model is consistent with earlier findings and provides an explanation for the role of L11(ntd) in elongation factor binding.
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