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Science 4 June 1993:
Vol. 260. no. 5113, pp. 1500 - 1503
DOI: 10.1126/science.8502993
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Articles

Science, Vol 260, Issue 5113, 1500-1503
Copyright © 1993 by American Association for the Advancement of Science

articles

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

U von Ahsen and HF Noller

Sinsheimer Laboratories, University of California, Santa Cruz 95064.

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.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Pentamidine inhibits catalytic activity of group I intron Ca.LSU by altering RNA folding.
Y. Zhang, Z. Li, D. S. Pilch, and M. J. Leibowitz (2002)
Nucleic Acids Res. 30, 2961-2971
   Abstract »    Full Text »    PDF »
A Small Protein (Ags1p) and the Pho80p-Pho85p Kinase Complex Contribute to Aminoglycoside Antibiotic Resistance of the Yeast Saccharomyces cerevisiae.
S. Wickert, M. Finck, B. Herz, and J. F. Ernst (1998)
J. Bacteriol. 180, 1887-1894
   Abstract »    Full Text »
Splice-site selection and decoding: are they related?.
R Schroeder, B Streicher, and H Wank (1993)
Science 260, 1443-1444
   PDF »


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