PMID:8034577
| Citation |
No author listed (1994) Analysis of the puromycin binding site in the 70 S ribosome of Escherichia coli at the peptide level. J. Biol. Chem. 269:18315-9 |
|---|---|
| Abstract |
Photoinduced cross-linking of Escherichia coli 70 S ribosomes with [3H]puromycin has led to the labeling of ribosomal proteins S7, S14, S18, L18, and L29. Proteolytic fragmentation of these proteins and separation of the peptide mixtures by C18 reversed-phase high performance liquid chromatography resulted in six puromycin-labeled peptides which were applied to sequence analysis. The following peptides were found labeled: Pro1-Lys10 of S7, Ala28-Lys46 and Ala7-Lys11 of S14, Asp24-Lys29 of S18, Tyr64-Lys68 of L18, and Thr55-Lys60 of L29. For the first time the molecular environment of an antibiotic in the procaryotic ribosome is presented at the peptide level. |
| Links | |
| Keywords |
Amino Acid Sequence; Binding Sites; Binding, Competitive; Chromatography, High Pressure Liquid; Escherichia coli/metabolism; Kinetics; Molecular Sequence Data; Peptide Fragments/chemistry; Peptide Fragments/metabolism; Puromycin/metabolism; Ribosomal Proteins/isolation & purification; Ribosomal Proteins/metabolism; Ribosomes/metabolism; Tritium |
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