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| Item Type: | Article |
|---|---|
| Title: | Peptide environment of the peptidyl transferase center from Escherichia coli 70 S ribosomes as determined by thermoaffinity labeling with dihydrospiramycin |
| Creators Name: | Bischof, O., Urlaub, H., Kruft, V. and Wittmann-Liebold, B. |
| Abstract: | In an attempt to gain information about the peptidyl transferase center at the peptide level we cross-linked the spiramycin derivative dihydrospiramycin to its functional binding site in the 70 S ribosome of Escherichia coli. In this manner ribosomal proteins S12, S14, L17, L18, L27 and L35 were found specifically affinity-labeled. Proteolytic fragmentation of these proteins, separation by C18 reversed-phase high performance liquid chromatography of the peptide mixtures, and subsequent sequence analysis of labeled peptides revealed peptide regions at positions Ala1-Lys9 and Tyr116-Lys119 of S12, Leu47-Asp53 of protein S14, Ser6-Lys35 of protein L17, Ala57-Lys63 of protein L18, Ala5-Lys18 and Val66-Lys71 of protein L27, and Thr5-Lys11 of protein L35. This approach is a valuable tool to characterize the binding site of spiramycin as well as the peptidyl transferase center at the molecular level. |
| Keywords: | Affinity Labels, Amino Acid Sequence, Anti-Bacterial Agents, Competitive Binding, Escherichia Coli, Kinetics, Molecular Sequence Data, Peptide Fragments, Peptidyl Transferases, Ribosomal Proteins, Ribosomes, Spiramycin |
| Source: | Journal of Biological Chemistry |
| ISSN: | 0021-9258 |
| Publisher: | American Society for Biochemistry and Molecular Biology |
| Volume: | 270 |
| Number: | 39 |
| Page Range: | 23060-23064 |
| Date: | 29 September 1995 |
| Official Publication: | https://doi.org/10.1074/jbc.270.39.23060 |
| PubMed: | View item in PubMed |
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