Journal ArticleDOI
Altered Ribosomal Protein in Streptomycin-Dependent Escherichia coli
Edward A. Birge,C. G. Kurland +1 more
TLDR
The 30S ribosomal proteins of strains of Escherichia coli sensitive to and dependent on streptomycin are compared and a single protein is identified that is functionally altered in the ribosomes dependent on Streptomytin.Abstract:
We have compared the 30S ribosomal proteins of strains of Escherichia coli sensitive to and dependent on streptomycin and identified a single protein that is functionally altered in the ribosomes dependent on streptomycin. This protein (30S-15) is the same protein that is functionally altered in ribosomes resistant to streptomycin.read more
Citations
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Journal ArticleDOI
Interaction of antibiotics with functional sites in 16S ribosomal RNA
Danesh Moazed,Harry F. Noller +1 more
TL;DR: Chemical footprinting shows that several classes of antibiotics protect concise sets of highly conserved nucleotides in 16S ribosomal RNA when bound to ribosomes, having strong implications for the mechanism of action of these antibiotics and for the assignment of functions to specific structural features of 16S rRNA.
Journal ArticleDOI
Assembly Mapping of 30S Ribosomal Proteins from E. coli
Shoji Mizushima,Masayasu Nomura +1 more
TL;DR: An assembly map of 30S ribosomal subunits has been constructed and it is shown that the assembly reaction is sequential and cooperative.
Journal ArticleDOI
Molecular basis of streptomycin resistance in Mycobacterium tuberculosis: alterations of the ribosomal protein S12 gene and point mutations within a functional 16S ribosomal RNA pseudoknot
TL;DR: It is demonstrated that streptomycin resistance is associated with mutations implicated in ribosomal resistance, and the mutations found either lead to amino acid changes in Ribosomal protein SI2 or alter the primary structure of the 16S rRNA.
Book ChapterDOI
[41] Reconstitution of ribosomes from subribosomal components
TL;DR: This chapter describes several techniques for the isolation of Escherichia coli ribosomes, and various methods for the dissociation of ribosomal subunits into their macromolecular constituents and for the reconstitution of Ribosomal particles from these constituents.
Journal ArticleDOI
RNA-protein interactions in 30S ribosomal subunits: folding and function of 16S rRNA
TL;DR: Several lines of evidence suggest that protein-dependent conformational changes in 16S rRNA play an important part in the cooperativity of ribosome assembly and in fine-tuning of the conformation and dynamics of 16SrRNA in the 30S subunit.
References
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Journal ArticleDOI
The ribosomal proteins of Escherichia coli. I. Purification of the 30S ribosomal proteins.
Journal ArticleDOI
Molecular characterization of ribonucleic acid from Escherichia coli ribosomes
TL;DR: The ribon nucleic acid from purified 30 s, 50 s and 70 s ribosomes of E. coli has been isolated by the phenol and detergent methods and it is suggested that they are heterogeneous; some contain one 23 s ribonucleic acid component, while others contain two 16 s units.
Journal ArticleDOI
Identification and Functional Characterization of the Protein controlled by the Streptomycin-resistant Locus in E. coli
TL;DR: The streptomycin locus of E. coli specifies a 30S ribosomal protein which determines the sensitivity of the 30S subunit to strePTomycin and streptomecin induced errors of translation.
Journal ArticleDOI
Structure and function of E. coli ribosomes. V. Reconstitution of functionally active 30S ribosomal particles from RNA and proteins.
TL;DR: Analysis of the activity of these particles has revealed the functional significance of each of the purified ribosomal split proteins, supporting the hypothesis of spontaneous self assembly.
Journal ArticleDOI
Antibiotic inhibitors of the bacterial ribosome.
Bernard Weisblum,Julian Davies +1 more
TL;DR: This article corrects the article on p. 493 in vol.
Related Papers (5)
Identification and Functional Characterization of the Protein controlled by the Streptomycin-resistant Locus in E. coli
Ribosomal proteins. 33. Location of amino-acid replacements in protein S12 isolated from Escherichia coli mutants resistant to streptomycin.
G Funatsu,H.G. Wittmann +1 more