Abstract
The antibiotic, micrococcin, binds to complexes, formed between bacterial 23‐S ribosomal RNA and ribosomal protein L11 and, in doing so, inhibits the binding of thiostrepton. In assay systems simulating partial reactions of protein synthesis, micrococcin inhibits a number of processes believed to involve the ribosomal A site while stimulating GTP hydrolysis dependent upon ribosomes and elongation factor EF‐G. The latter effect is not observed upon ribosomes lacking a protein homologous with protein L11. Nor is it apparent upon those containing 23‐S RNA previously subjected to the action of a specific methylase known to render ribosomes resistant to thiostrepton. It is concluded that stimulation by micrococcin of factor‐dependent GTP hydrolysis results from the binding of the drug to its normal target site which involves 23‐S RNA and protein L11.
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Dates
Type | When |
---|---|
Created | 20 years, 5 months ago (March 3, 2005, 4:15 p.m.) |
Deposited | 1 year, 9 months ago (Nov. 23, 2023, 2:18 a.m.) |
Indexed | 1 month, 4 weeks ago (July 2, 2025, 2:46 p.m.) |
Issued | 44 years ago (Aug. 1, 1981) |
Published | 44 years ago (Aug. 1, 1981) |
Published Online | 20 years, 5 months ago (March 3, 2005) |
Published Print | 44 years ago (Aug. 1, 1981) |
@article{CUNDLIFFE_1981, title={Concerning the Mode of Action of Micrococcin upon Bacterial Protein Synthesis}, volume={118}, ISSN={1432-1033}, url={http://dx.doi.org/10.1111/j.1432-1033.1981.tb05484.x}, DOI={10.1111/j.1432-1033.1981.tb05484.x}, number={1}, journal={European Journal of Biochemistry}, publisher={Wiley}, author={CUNDLIFFE, Eric and THOMPSON, Jill}, year={1981}, month=aug, pages={47–52} }