E. coli ribosomes with a C912 to U base change in the 16S rRNA are streptomycin resistant.

Montandon, Paul-Etienne; Wagner, Rolf; Stutz, Erhard

doi:10.1002/j.1460-2075.1986.tb04703.x

Cited by 97 publications

(51 citation statements)

References 27 publications

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“…Streptomycin does not appear to bind to the S12 protein itself, but rather it binds to S12-deficient ribosomal core particles, and other proteins such as S3 and S5 are required (50). In E. coli, two streptomycin binding sites (positions 912 and 523) have been identified within 16S rRNA (36,38). Position 912 is adjacent to the S12 and S5 proteins, while position 523 is adjacent to the S4 protein (reviewed by Noller et al [39]).…”

Section: Discussionmentioning

confidence: 99%

Induction of actinorhodin production by rpsL (encoding ribosomal protein S12) mutations that confer streptomycin resistance in Streptomyces lividans and Streptomyces coelicolor A3(2)

et al. 1996

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A strain of Streptomyces lividans, TK24, was found to produce a pigmented antibiotic, actinorhodin, although S. lividans normally does not produce this antibiotic. Genetic analyses revealed that a streptomycin-resistant mutation str-6 in strain TK24 is responsible for induction of antibiotic synthesis. DNA sequencing showed that str-6 is a point mutation in the rpsL gene encoding ribosomal protein S12, changing Lys-88 to Glu. Gene replacement experiments with the Lys883Glu str allele demonstrated unambiguously that the str mutation is alone responsible for the activation of actinorhodin production observed. In contrast, the strA1 mutation, a genetic marker frequently used for crosses, did not restore actinorhodin production and was found to result in an amino acid alteration of Lys-43 to Asn. Induction of actinorhodin production was also detected in strain TK21, which does not harbor the str-6 mutation, when cells were incubated with sufficient streptomycin or tetracycline to reduce the cell's growth rate, and 40 and 3% of streptomycin-or tetracycline-resistant mutants, respectively, derived from strain TK21 produced actinorhodin. Streptomycin-resistant mutations also blocked the inhibitory effects of relA and brgA mutations on antibiotic production, aerial mycelium formation or both. These str mutations changed Lys-88 to Glu or Arg and Arg-86 to His in ribosomal protein S12. The decrease in streptomycin production in relC mutants in Streptomyces griseus could also be abolished completely by introducing streptomycin-resistant mutations, although the impairment in antibiotic production due to bldA (in Streptomyces coelicolor) or afs mutations (in S. griseus) was not eliminated. These results indicate that the onset and extent of secondary metabolism in Streptomyces spp. is significantly controlled by the translational machinery.

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Section: Discussionmentioning

confidence: 99%

Induction of actinorhodin production by rpsL (encoding ribosomal protein S12) mutations that confer streptomycin resistance in Streptomyces lividans and Streptomyces coelicolor A3(2)

et al. 1996

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“…No variation in this composition was observed in oligonucleotide catalogs (about 400 species [48]), and the indicated C residue distinguishes eubacteria from archaebacteria and eucaryotes (42), all of which showed a U residue at this position (position 912). It has been reported that a mutation that changes this C residue to a U residue (in Escherichia coli) confers streptomycin resistance (20). The only known example of a C residue at this position among the naturally streptomycin-resistant archaebacteria occurs in Desulfurococcus mobilis, the only archaebacterium that is sensitive to streptomycin (R. Garrett, personal communication …”

Section: And Discussionmentioning

confidence: 99%

A phylogenetic analysis of the mycoplasmas: basis for their classification

et al. 1989

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Small-subunit rRNA sequences were determined for almost 50 species of mycoplasmas and their walled relatives, providing the basis for a phylogenetic systematic analysis of these organisms. Five groups of mycoplasmas per se were recognized (provisional names are given): the hominis group (which included species such as Mycoplasma hominis, Mycoplasma lipophilum, Mycoplasma pulmonis, and Mycoplasma neurolyticum), the pneumoniae group (which included species such as Mycoplasma pneumoniae and Mycoplasma muris), the spiroplasma group (which included species such as Mycoplasma mycoides, Spiroplasma citri, and Spiroplasma apis), the anaeroplasma group (which encompassed the anaeroplasmas and acholeplasmas), and a group known to contain only the isolated species Asteroleplasma anaerobium. In addition to these five mycoplasma groups, a sixth group of variously named gram-positive, walled organisms (which included lactobacilli, clostridia, and other organisms) was also included in the overall phylogenetic unit. In each of these six primary groups, subgroups were readily recognized and defined. Although the phylogenetic units identified by rRNA comparisons are difficult to recognize on the basis of mutually exclusive phenotypic characters alone, phenotypic justification can be given a posteriori for a number of them.

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“…Despite this difference, streptomycin binds at the functional center of the ribosome in close proximity to the binding site of paromomycin. Tight binding of antibiotic is facilitated by interaction with nucleotides 13, 526, 915, and 1490 of 16S rRNA and protein S12 (45, 105,186,191,196). Like 2-deoxystreptamine-containing aminoglycosides, streptomycin induces misreading of the genetic code (142,143,250), but the underlying mechanism seems to be different.…”

Section: Mechanism Of Actionmentioning

confidence: 99%

Versatility of Aminoglycosides and Prospects for Their Future

2003

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Aminoglycoside antibiotics have had a major impact on our ability to treat bacterial infections for the past half century. Whereas the interest in these versatile antibiotics continues to be high, their clinical utility has been compromised by widespread instances of resistance. The multitude of mechanisms of resistance is disconcerting but also illuminates how nature can manifest resistance when bacteria are confronted by antibiotics. This article reviews the most recent knowledge about the mechanisms of aminoglycoside action and the mechanisms of resistance to these antibiotics

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E. coli ribosomes with a C912 to U base change in the 16S rRNA are streptomycin resistant.

Cited by 97 publications

References 27 publications

Induction of actinorhodin production by rpsL (encoding ribosomal protein S12) mutations that confer streptomycin resistance in Streptomyces lividans and Streptomyces coelicolor A3(2)

Induction of actinorhodin production by rpsL (encoding ribosomal protein S12) mutations that confer streptomycin resistance in Streptomyces lividans and Streptomyces coelicolor A3(2)

A phylogenetic analysis of the mycoplasmas: basis for their classification

Versatility of Aminoglycosides and Prospects for Their Future

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