Thiostrepton resistance mutations in the gene for 23S ribosomal RNA of Halobacteria

Chloramphenicol resistance mutations in the single 23S rRNA gene of the archaeon Halobacterium halobium

“…Spontaneous single-point mutants with a chloramphenicol-resistant phenotype arose in halobacterial cultures with a frequency of about 10-7. This is close to the frequencies observed for thiostreptonor anisomycin-resistant mutants, which are also characterized by single-nucleotide substitutions in the 23S rRNA gene (11,12), and this probably corresponds to the mutation rate of the H. halobium genome.…”

Chloramphenicol resistance mutations in the single 23S rRNA gene of the archaeon Halobacterium halobium

“…Spontaneous single-point mutants with a chloramphenicol-resistant phenotype arose in halobacterial cultures with a frequency of about 10-7. This is close to the frequencies observed for thiostreptonor anisomycin-resistant mutants, which are also characterized by single-nucleotide substitutions in the 23S rRNA gene (11,12), and this probably corresponds to the mutation rate of the H. halobium genome.…”

Phenotypic Suppression of Streptomycin Resistance by Mutations in Multiple Components of the Translation Apparatus

“…The peptide antibiotic thiostrepton acts by binding to the GTPase-associated center (GAC) of the 50S subunit at a cleft formed by the N-terminal domain (NTD) of ribosomal protein L11 and helices 43 and 44 of 23S rRNA (38). Resistance to thiostrepton can be conferred by base substitutions in 23S rRNA (39,40) or amino acid substitutions in L11 (41). While it is known primarily as an inhibitor of translocation (reviewed in reference 1), thiostrepton has also been shown to interfere with formation of a stable complex between the ribosome and EF-Tu-GTP-aminoacyl-tRNA (aa-tRNA) (42).…”

In vitro and intracellular activities of novel thiopeptide derivatives against macrolide-susceptible and macrolide-resistant Mycobacterium avium complex

“…Our results highlight that there is no cross-resistance between thiopeptide derivatives and CLR, even though they both target bacterial ribosomes. It has been reported in other species that resistance to thiopeptide is associated with mutations in H43 and H44 of the 23S rRNA or in rplk , a gene encoding ribosomal protein L11 ( 54 – 56 ). Moreover, thiopeptides are active against many antibiotic-resistant bacteria, such as MRSA, vancomycin-resistant enterococci, and penicillin-resistant Streptococcus pneumonia ( 16 , 24 ).…”

Chloramphenicol resistance mutations in the single 23S rRNA gene of the archaeon Halobacterium halobium

“…Spontaneous single-point mutants with a chloramphenicol-resistant phenotype arose in halobacterial cultures with a frequency of about 10-7. This is close to the frequencies observed for thiostreptonor anisomycin-resistant mutants, which are also characterized by single-nucleotide substitutions in the 23S rRNA gene (11,12), and this probably corresponds to the mutation rate of the H. halobium genome.…”

Phenotypic Suppression of Streptomycin Resistance by Mutations in Multiple Components of the Translation Apparatus

“…The peptide antibiotic thiostrepton acts by binding to the GTPase-associated center (GAC) of the 50S subunit at a cleft formed by the N-terminal domain (NTD) of ribosomal protein L11 and helices 43 and 44 of 23S rRNA (38). Resistance to thiostrepton can be conferred by base substitutions in 23S rRNA (39,40) or amino acid substitutions in L11 (41). While it is known primarily as an inhibitor of translocation (reviewed in reference 1), thiostrepton has also been shown to interfere with formation of a stable complex between the ribosome and EF-Tu-GTP-aminoacyl-tRNA (aa-tRNA) (42).…”

In vitro and intracellular activities of novel thiopeptide derivatives against macrolide-susceptible and macrolide-resistant Mycobacterium avium complex

“…Our results highlight that there is no cross-resistance between thiopeptide derivatives and CLR, even though they both target bacterial ribosomes. It has been reported in other species that resistance to thiopeptide is associated with mutations in H43 and H44 of the 23S rRNA or in rplk , a gene encoding ribosomal protein L11 ( 54 – 56 ). Moreover, thiopeptides are active against many antibiotic-resistant bacteria, such as MRSA, vancomycin-resistant enterococci, and penicillin-resistant Streptococcus pneumonia ( 16 , 24 ).…”

Chloramphenicol resistance mutations in the single 23S rRNA gene of the archaeon Halobacterium halobium

“…Spontaneous single-point mutants with a chloramphenicol-resistant phenotype arose in halobacterial cultures with a frequency of about 10-7. This is close to the frequencies observed for thiostreptonor anisomycin-resistant mutants, which are also characterized by single-nucleotide substitutions in the 23S rRNA gene (11,12), and this probably corresponds to the mutation rate of the H. halobium genome.…”

Phenotypic Suppression of Streptomycin Resistance by Mutations in Multiple Components of the Translation Apparatus

“…The peptide antibiotic thiostrepton acts by binding to the GTPase-associated center (GAC) of the 50S subunit at a cleft formed by the N-terminal domain (NTD) of ribosomal protein L11 and helices 43 and 44 of 23S rRNA (38). Resistance to thiostrepton can be conferred by base substitutions in 23S rRNA (39,40) or amino acid substitutions in L11 (41). While it is known primarily as an inhibitor of translocation (reviewed in reference 1), thiostrepton has also been shown to interfere with formation of a stable complex between the ribosome and EF-Tu-GTP-aminoacyl-tRNA (aa-tRNA) (42).…”

In vitro and intracellular activities of novel thiopeptide derivatives against macrolide-susceptible and macrolide-resistant Mycobacterium avium complex

“…Our results highlight that there is no cross-resistance between thiopeptide derivatives and CLR, even though they both target bacterial ribosomes. It has been reported in other species that resistance to thiopeptide is associated with mutations in H43 and H44 of the 23S rRNA or in rplk , a gene encoding ribosomal protein L11 ( 54 – 56 ). Moreover, thiopeptides are active against many antibiotic-resistant bacteria, such as MRSA, vancomycin-resistant enterococci, and penicillin-resistant Streptococcus pneumonia ( 16 , 24 ).…”