PMID:6759118
| Citation |
Riehl, N, Remy, P, Ebel, JP and Ehresmann, B (1982) Crosslinking of N-acetyl-phenylalanyl [s4U]tRNAPhe to protein S10 in the ribosomal P site. Eur. J. Biochem. 128:427-33 |
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| Abstract |
In order to identify ribosomal components involved in the peptidyl-tRNA binding site on the ribosome, tRNAPhe molecules were prepared in which cytidine residues had been chemically converted into 4-thiouridine (S4U). This nucleoside is photoactive at 335 nm and able to form covalent bonds with nearby nucleophilic groups. The thiolated AcPhe-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. |
| Links | |
| Keywords |
Base Sequence; Escherichia coli/metabolism; Kinetics; Nucleic Acid Conformation; Phenylalanine-tRNA Ligase/metabolism; RNA, Transfer, Amino Acyl/metabolism; Ribosomal Proteins/metabolism; Ribosomes/metabolism; Saccharomyces cerevisiae/enzymology; Spectrophotometry, Ultraviolet |
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