Literature DB >> 9195872

In vitro selection of a viomycin-binding RNA pseudoknot.

M G Wallis1, B Streicher, H Wank, U von Ahsen, E Clodi, S T Wallace, M Famulok, R Schroeder.   

Abstract

BACKGROUND: The peptide antibiotic viomycin inhibits ribosomal protein synthesis, group I intron self-splicing and self-cleavage of the human hepatitis delta virus ribozyme. To understand the molecular basis of RNA binding and recognition by viomycin, we isolated a variety of novel viomycin-binding RNA molecules using in vitro selection.
RESULTS: More than 90% of the selected RNA molecules shared one continuous highly conserved region of 14 nucleotides. Mutational analyses, structural probing, together with footprinting experiments by chemical modification, and Pb2+-induced cleavage showed that this conserved sequence harbours the antibiotic-binding site and forms a stem-loop structure. Moreover, the loop is engaged in a long-range interaction forming a pseudoknot.
CONCLUSIONS: A comparison between the novel viomycin-binding motif and the natural RNA target sites for viomycin showed that all these segments form a pseudoknot at the antibiotic-binding site. We therefore conclude that this peptide antibiotic has a strong selectivity for particular RNA pseudoknots.

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Year:  1997        PMID: 9195872     DOI: 10.1016/s1074-5521(97)90126-5

Source DB:  PubMed          Journal:  Chem Biol        ISSN: 1074-5521


  11 in total

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6.  Vitamin B12 and hepatitis C: molecular biology and human pathology.

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7.  In vitro selection and characterization of streptomycin-binding RNAs: recognition discrimination between antibiotics.

Authors:  S T Wallace; R Schroeder
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8.  The antibiotic viomycin as a model peptide for the origin of the co-evolution of RNA and proteins.

Authors:  H Wank; E Clodi; M G Wallis; R Schroeder
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9.  Aptamers for pharmaceuticals and their application in environmental analytics.

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10.  Challenges and opportunities for small molecule aptamer development.

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