ArticleJournal of bacteriology1992
Functional interactions within 23S rRNA involving the peptidyltransferase center.
Article in Journal of bacteriology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 95 citations in OpenAlex.
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- Intercepting biological messages: Antibacterial molecules targeting nucleic acids during interbacterial conflicts.Genetics and molecular biology · 2023Article
- Targeted editing and evolution of engineered ribosomes in vivo by filtered editing.Nature communications · 2022Article
- New Chloramphenicol Derivatives from the Viewpoint of Anticancer and Antimicrobial Activity.Antibiotics (Basel, Switzerland) · 2019Article
- Lincosamides, Streptogramins, Phenicols, and Pleuromutilins: Mode of Action and Mechanisms of Resistance.Cold Spring Harbor perspectives in medicine · 2016Review
- Resistance to Macrolide Antibiotics in Public Health Pathogens.Cold Spring Harbor perspectives in medicine · 2016Review
- Development and characterisation of highly antibiotic resistant Bartonella bacilliformis mutants.Scientific reports · 2016Article
- Chloramphenicol Derivatives as Antibacterial and Anticancer Agents: Historic Problems and Current Solutions.Antibiotics (Basel, Switzerland) · 2016Review
- Synthesis and evaluation of chloramphenicol homodimers: molecular target, antimicrobial activity, and toxicity against human cells.PloS one · 2015Article
- Antibiotic drugs targeting bacterial RNAs.Acta pharmaceutica Sinica. B · 2014Review
- Conjugation with polyamines enhances the antibacterial and anticancer activity of chloramphenicol.Nucleic acids research · 2014Article
- Identification of a novel G2073A mutation in 23S rRNA in amphenicol-selected mutants of Campylobacter jejuni.PloS one · 2014Article
- Tools for characterizing bacterial protein synthesis inhibitors.Antimicrobial agents and chemotherapy · 2013Article
- Trends towards lower antimicrobial susceptibility and characterization of acquired resistance among clinical isolates of Brachyspira hyodysenteriae in Spain.Antimicrobial agents and chemotherapy · 2011Article
- High-level azithromycin resistance occurs in Neisseria gonorrhoeae as a result of a single point mutation in the 23S rRNA genes.Antimicrobial agents and chemotherapy · 2010Article
- Structural basis for cross-resistance to ribosomal PTC antibiotics.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Protein folding by domain V of Escherichia coli 23S rRNA: specificity of RNA-protein interactions.Journal of bacteriology · 2008Article
- Responses of wild-type and resistant strains of the hyperthermophilic bacterium Thermotoga maritima to chloramphenicol challenge.Applied and environmental microbiology · 2007Article
- Mutational analysis of 16S and 23S rRNA genes of Thermus thermophilus.Journal of bacteriology · 2005Article
- A conserved chloramphenicol binding site at the entrance to the ribosomal peptide exit tunnel.Nucleic acids research · 2003Article
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1 author.
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No grant is acknowledged in the PubMed record.
Abstract
A molecular genetic approach has been employed to investigate functional interactions within 23S rRNA. Each of the three base substitutions at guanine 2032 has been made. The 2032A mutation confers resistance to the antibiotics chloramphenicol and clindamycin, which interact with the 23S rRNA peptidyltransferase loop. All three base substitutions at position 2032 produce an erythromycin-hypersensitive phenotype. The 2032 substitutions were compared with and combined with a 12-bp deletion mutation in domain II and point mutations at positions 2057 and 2058 in the peptidyltransferase region of domain V that also confer antibiotic resistance. Both the domain II deletion and the 2057A mutation relieve the hypersensitive effect of the 2032A mutation, producing an erythromycin-resistant phenotype; in addition, the combination of the 2032A and 2057A mutations confers a higher level of chloramphenicol resistance than either mutation alone. 23S rRNAs containing mutations at position 2058 that confer clindamycin and erythromycin resistance become deleterious to cell growth when combined with the 2032A mutation and, additionally, confer hypersensitivity to erythromycin and sensitivity to clindamycin and chloramphenicol. Introduction of the domain II deletion into these double-mutation constructs gives rise to erythromycin resistance. The results are interpreted as indicating that position 2032 interacts with the peptidyltransferase loop and that there is a functional connection between domains II and V.
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