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Published online 17 May 2004

Nucleic Acids Research, 2004, Vol. 32, No. 9 2707-2715
© 2004 Oxford University Press

A three-fluorophore FRET assay for high-throughput screening of small-molecule inhibitors of ribosome assembly

Dagmar Klostermeier1, Pamela Sears2, Chi-Huey Wong2, David P. Millar1 and James R. Williamson*,1,2

1 The Scripps Research Institute, Department of Molecular Biology and 2 Department of Chemistry and The Skaggs Institute for Chemical Biology, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA

*To whom correspondence should be addressed. Tel: +1 858 784 8740; Fax: +1 858 784 2199; Email: jrwill{at}scripps.edu
Present address:
D. Klostermeier, Department of Experimental Physics IV, Universitätsstraße 30, 95440 Bayreuth, Germany

Received January 26, 2004; Revised and Accepted April 15, 2004

In one of the first steps of prokaryotic ribosome assembly, the ribosomal protein S15 binds to a three-way junction in the central domain of the 16S rRNA. Binding causes a conformational change that is required for subsequent binding events. Using a novel fluorescence resonance energy transfer assay with three fluorophores, two on the RNA and one on the S15 protein, small-molecule libraries can be screened for potential inhibitors of this initial step in ribosome assembly. The employment of three fluorophores allows both the conformational change of the RNA and the binding of S15 to be monitored in a single assay.


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