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Peptide environment of the peptidyl transferase center from Escherichia coli 70 S ribosomes as determined by thermoaffinity labeling with dihydrospiramycin

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. and Urlaub, H. and 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 (U.S.A.)
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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