Streptomycin Resistance Mutation in Escherichia coli : Altered Ribosomal Protein
- 12 April 1968
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 160 (3824), 198-199
- https://doi.org/10.1126/science.160.3824.198
Abstract
Reconstitution of 30S ribosomal particles was performed with 16S ribosomal RNA, "core" proteins, and "split" proteins from 30S particles derived from streptomycin-sensitive and streptomycin-resistant Escherichia coli cells in various combinations. Analysis of streptomycin sensitivity of the reconstituted particles has shown that the alteration induced by the resistance mutation resides in the core proteins, and not in the RNA or in the split proteins of the 30S particles.This publication has 10 references indexed in Scilit:
- Structure and functior of Escherichia coli ribosomesJournal of Molecular Biology, 1968
- Structure and function of E. coli ribosomes. V. Reconstitution of functionally active 30S ribosomal particles from RNA and proteins.Proceedings of the National Academy of Sciences, 1968
- Determination of streptomycin sensitivity by a subunit of the 30 s ribosome of Escherichia coliJournal of Molecular Biology, 1966
- Physical and functional heterogeneity of ribosomal proteinsJournal of Molecular Biology, 1966
- Reconstitution of functionally active ribosomes from inactive subparticles and proteins.Proceedings of the National Academy of Sciences, 1966
- Mutations and Genetics Concerned With the RibosomeCold Spring Harbor Symposia on Quantitative Biology, 1966
- STREPTOMYCIN, SUPPRESSION, AND THE CODEProceedings of the National Academy of Sciences, 1964
- Conservation of ribosomes during bacterial growthJournal of Molecular Biology, 1964
- Polypeptide synthesis with ribosomes from streptomycin-resistant and dependent E.coliBiochemical and Biophysical Research Communications, 1962
- Mechanism of Streptomycin Action on Bacteria: A Unitary HypothesisNature, 1961