Crosslinking of N‐Acetyl‐phenylalanyl [s4U]tRNAPhe to Protein S10 in the Ribosomal P Site
Open Access
- 1 November 1982
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 128 (2-3) , 427-433
- https://doi.org/10.1111/j.1432-1033.1982.tb06982.x
Abstract
In order to identify ribosomal components involved in the peptidyl-tRNA binding site on the ribosome [yeast], tRNAPhe molecules were prepared in which cytidine residues had been chemically converted into 4-thiouridine (s4U). This nucleotide is photoactive at 335 nm and able to form covalent bonds with nearby nucleophilic groups. The thiolated AcPhe-tRNAPhe [N-acetylphenylalanyl-[4-thiouridine]tRNAPhe] was bound to the ribosomal P site in the presence of poly(U) as verified by puromycin reactivity. Direct irradiation of the AcPhe-[s4U]tRNAPhe/poly(U)/70-S ribosome complex induced crosslinking of the tRNA molecule exclusively to 30-S subunits. Analysis of the covalent complex revealed that AcPhe-[s4U]tRNAPhe was specifically crosslinked to protein S10.This publication has 31 references indexed in Scilit:
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