ArticleNature structural & molecular biology2006
The electrostatic character of the ribosomal surface enables extraordinarily rapid target location by ribotoxins.
Article in Nature structural & molecular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- Review
- Heterologous Production and Functional Characterization of Ageritin, a Novel Type of Ribotoxin Highly Expressed during Fruiting of the Edible Mushroom Agrocybe aegerita.Applied and environmental microbiology · 2019Article
- Concerted 2-5A-Mediated mRNA Decay and Transcription Reprogram Protein Synthesis in the dsRNA Response.Molecular cell · 2019Article
- Enhancement of RNA/Ligand Association Kinetics via an Electrostatic Anchor.Biochemistry · 2019Article
- Distributive enzyme binding controlled by local RNA context results in 3' to 5' directional processing of dicistronic tRNA precursors by Escherichia coli ribonuclease P.Nucleic acids research · 2019Article
- Human ribosomal P1-P2 heterodimer represents an optimal docking site for ricin A chain with a prominent role for P1 C-terminus.Scientific reports · 2017Article
- Ricin uses arginine 235 as an anchor residue to bind to P-proteins of the ribosomal stalk.Scientific reports · 2017Article
- Review
- Structures and Ribosomal Interaction of Ribosome-Inactivating Proteins.Molecules (Basel, Switzerland) · 2016Review
- Ensemble cryo-EM uncovers inchworm-like translocation of a viral IRES through the ribosome.eLife · 2016Article
- Solution structure of the Z-DNA binding domain of PKR-like protein kinase from Carassius auratus and quantitative analyses of the intermediate complex during B-Z transition.Nucleic acids research · 2016Article
- Arginine residues on the opposite side of the active site stimulate the catalysis of ribosome depurination by ricin A chain by interacting with the P-protein stalk.The Journal of biological chemistry · 2013Article
- Quantitative analysis of multisite protein-ligand interactions by NMR: binding of intrinsically disordered p53 transactivation subdomains with the TAZ2 domain of CBP.Journal of the American Chemical Society · 2012Article
- Interaction of ricin and Shiga toxins with ribosomes.Current topics in microbiology and immunology · 2012Review
- Charged and hydrophobic surfaces on the a chain of shiga-like toxin 1 recognize the C-terminal domain of ribosomal stalk proteins.PloS one · 2012Article
- The ribotoxin restrictocin recognizes its RNA substrate by selective engagement of active site residues.Biochemistry · 2011Article
- Small-molecule inhibitor leads of ribosome-inactivating proteins developed using the doorstop approach.PloS one · 2011Article
- Identification of amino acids critical for the cytotoxicity of Shiga toxin 1 and 2 in Saccharomyces cerevisiae.Toxicon : official journal of the International Society on Toxinology · 2011Article
- Pentameric organization of the ribosomal stalk accelerates recruitment of ricin a chain to the ribosome for depurination.The Journal of biological chemistry · 2010Article
- Cleavage of the sarcin-ricin loop of 23S rRNA differentially affects EF-G and EF-Tu binding.Nucleic acids research · 2010Article
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3 authors.
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Abstract
Alpha-sarcin ribotoxins comprise a unique family of ribonucleases that cripple the ribosome by catalyzing endoribonucleolytic cleavage of ribosomal RNA at a specific location in the sarcin/ricin loop (SRL). The SRL structure alone is cleaved site-specifically by the ribotoxin, but the ribosomal context enhances the reaction rate by several orders of magnitude. We show that, for the alpha-sarcin-like ribotoxin restrictocin, this catalytic advantage arises from favorable electrostatic interactions with the ribosome. Restrictocin binds at many sites on the ribosomal surface and under certain conditions cleaves the SRL with a second-order rate constant of 1.7 x 10(10) M(-1) s(-1), a value that matches the predicted frequency of random restrictocin-ribosome encounters. The results suggest a mechanism of target location whereby restrictocin encounters ribosomes randomly and diffuses within the ribosomal electrostatic field to the SRL. These studies show a role for electrostatics in protein-ribosome recognition.
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