Identification of a 16‐S RNA Fragment Crosslinked to Protein S1 within Escherichia coli Ribosomal 30‐S Subunits by the Use of a Crosslinking Reagent: Ethyl 4‐Azidobenzoylaminoacetimidate

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Abstract

The bifunctional reagent ethyl 4‐azidobenzoylaminoacetimidate was used to crosslink specifically ribosomal protein S1 to 16‐S RNA within 30‐S subunits. The reagent was attached to isolated protein S1. The modified protein was reassociated with protein‐SI‐depleted 30‐S subunits and then crosslinked to the RNA molecule. The covalently bound 16‐S RNA‐protein S1 complex was isolated and the RNA fragment C‐U‐A‐A‐C‐G‐C‐G‐U‐U‐A‐A‐G‐U‐C‐G‐A‐C‐C‐G‐C‐C‐U‐G‐G‐G‐G‐A‐G (positions 861–889) was characterized to be crosslinked to protein S1. Copyright © 1981, Wiley Blackwell. All rights reserved

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GOLINSKA, B., MILLON, R., BACKENDORF, C., EBEL, J. ‐P, EHRESMANN, B., & OLOMUCKI, M. (1981). Identification of a 16‐S RNA Fragment Crosslinked to Protein S1 within Escherichia coli Ribosomal 30‐S Subunits by the Use of a Crosslinking Reagent: Ethyl 4‐Azidobenzoylaminoacetimidate. European Journal of Biochemistry, 115(3), 479–484. https://doi.org/10.1111/j.1432-1033.1981.tb06227.x

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