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Footprinting the sites of interaction of antibiotics with catalytic group I intron RNA.

Authors
Type
Published Article
Journal
Science
Publisher
American Association for the Advancement of Science (AAAS)
Volume
260
Issue
5113
Pages
1500–1503
Source
UCSC Bioinformatics biomedical-ucsc
License
Unknown

Abstract

Aminoglycoside inhibitors of translation have been shown previously to inhibit in vitro self-splicing by group I introns. Chemical probing of the phage T4-derived sunY intron shows that neomycin, streptomycin, and related antibiotics protected the N-7 position of G96, a universally conserved guanine in the binding site for the guanosine cofactor in the splicing reaction. The antibiotics also disrupted structural contacts that have been proposed to bring the 5 cleavage site of the intron into proximity to the catalytic core. In contrast, the strictly competitive inhibitors deoxyguanosine and arginine protected only the N-7 position of G96. Parallels between these results and previously observed protection of 16S ribosomal RNA by aminoglycosides raise the possibility that group I intron splicing and transfer RNA selection by ribosomes involve similar RNA structural motifs.

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