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

Dagmar Klostermeier | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

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

Author(s) -

Dagmar Klostermeier

Publication year - 2004

Publication title -

nucleic acids research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 9.008

H-Index - 537

eISSN - 1362-4954

pISSN - 0305-1048

DOI - 10.1093/nar/gkh588

Subject(s) - ribosome , förster resonance energy transfer , biology , fluorophore , conformational change , 5.8s ribosomal rna , ribosomal rna , single molecule fret , biophysics , small molecule , translation (biology) , rna , ribosomal protein , biochemistry , microbiology and biotechnology , fluorescence , messenger rna , gene , physics , quantum mechanics

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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research