The Photochemical Inactivation of Peptidyl Transferase Activity
- 1 October 1975
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 58 (2), 397-402
- https://doi.org/10.1111/j.1432-1033.1975.tb02386.x
Abstract
The photochemical oxidation of the 50-S ribosomal subunit results in a rapid irreversible loss of peptidyl transferase activity. The first-order rate of inactivation occurring during the first forty minutes suggests that a single reactive group is being inactivation exhibits a maximum at pH 7.5. Erythromycin at a low concentration (0.04 mumol) affords significant protection. Puromycin also exerts a protective effect but at higher concentrations. Chloramphenicol, sparsomycin and lincomycin did not exert a protective effect. The loss in catalytic activity was not accompanied by a loss in substrate binding affinity of the donor and acceptor substrates.Keywords
This publication has 27 references indexed in Scilit:
- Inhibitors of protein synthesisFEBS Letters, 1974
- Chemical modification of the transfer RNA and polyuridylic acid binding sites of Escherichia coli 30 s ribosomal subunitsJournal of Molecular Biology, 1971
- Correlation between the peptidyl transferase activity of the 50 s ribosomal subunit and the ability of the subunit to interact with antibioticsJournal of Molecular Biology, 1971
- Substrate and antibiotic binding sites at the peptidyl transferase centre of E. coli ribosomes: Binding of UACCA‐Leu to 50 S subunitsFEBS Letters, 1971
- Inactivation and reactivation of ribosomal subunits: The peptidyl transferase activity of the 50 s subunit of Escherichia coliJournal of Molecular Biology, 1970
- Substrate and antibiotic binding sites at the peptidyl transferase centre of E. coli ribosomesFEBS Letters, 1970
- Interconversions between inactive and active forms of ribosomal subunitsFEBS Letters, 1969
- The inactivation and reactivation of ribosomal-peptidyl transferase of E. coliBiochemical and Biophysical Research Communications, 1968
- Catalysis of peptide bond formation by 50 s ribosomal subunits from Escherichia coliJournal of Molecular Biology, 1967
- Initiation of protein synthesis II a convenient assay for the ribosome-dependent synthesis of N-formyl-C14-methionylpuromycinBiochemical and Biophysical Research Communications, 1966