The chemical modification of Escherichia coli ribosomes with methyl p-nitrobenzenesulfonate. Evidence for the involvement of a histidine residue in the functioning of the ribosomal peptidyl transferase
- 1 December 1980
- journal article
- research article
- Published by Canadian Science Publishing in Canadian Journal of Biochemistry
- Vol. 58 (12), 1345-1347
- https://doi.org/10.1139/o80-182
Abstract
Free 70S ribosomes and 70S ribosome-AUG-fMet-tRNA complexes were reacted, separately with methyl p-nitrobenzenesulfonate. This reagent inhibits the peptidyl transferase activity of 70S ribosome-AUG-fMet-tRNA but not of free 70S ribosomes. Methyl p-nitrobenzenesulfonate apparently reacts with a unique site which is a part of the ribosomal peptidyl transferase.This publication has 6 references indexed in Scilit:
- A molecular model of peptide chain propagationJournal of Theoretical Biology, 1980
- Peptide Bond Formation Stimulated by Protein Synthesis Factor EF‐P Depends on the Aminoacyl Moiety of the AcceptorEuropean Journal of Biochemistry, 1979
- Purification of factor EF-P, a protein that stimulates peptide-bond synthesis with certain aminoacyl-tRNA analoguesCanadian Journal of Biochemistry, 1979
- The Modification of the Peptidyl Transferase Activity of 50-S Ribosomal Subunits, LiCl-Split Proteins and L16 Ribosomal Protein by Ethoxyformic AnhydrideEuropean Journal of Biochemistry, 1978
- Characterization and Site of Action of a Soluble Protein that Stimulates Peptide‐Bond SynthesisEuropean Journal of Biochemistry, 1976
- Factor-free (“Non-enzymic”) and factor-dependent systems of translation of polyuridylic acid by Escherichia coli ribosomesJournal of Molecular Biology, 1976