Functional interactions within 23S rRNA involving the peptidyltransferase center.

doi:10.1128/jb.174.4.1333-1338.1992

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Article

Functional interactions within 23S rRNA involving the peptidyltransferase center.

Journal of bacteriology - 1 Feb 1992

Douthwaite S

Abstract excerpt

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....

Topics

Bacteriophage lambda
Base Composition
Base Sequence
Chloramphenicol Resistance
Clindamycin
DNA Mutational Analysis
Drug Resistance, Microbial
Erythromycin
Escherichia coli
Molecular Sequence Data
Mutagenesis, Site-Directed

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Nucleic Acid Conformation

Peptidyl Transferases

Plasmids

Promoter Regions, Genetic

RNA, Ribosomal, 23S

Source

Open in PubMed Open full text

Identifiers

PMID: 1531223
DOI: 10.1128/jb.174.4.1333-1338.1992
PMCID: PMC206429

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1531223-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Functional interactions within 23S rRNA involving the peptidyltransferase center.PMID 1531223Read ↗

Erythromycin binding is reduced in ribosomes with conformational alterations in the 23 S rRNA peptidyl transferase loop.Semantic proximity Read ↗

Mutations at nucleotides G2251 and U2585 of 23 S rRNA perturb the peptidyl transferase center of the ribosome.Semantic proximity Read ↗

Mutations in domain II of 23 S rRNA facilitate translation of a 23 S rRNA-encoded pentapeptide conferring erythromycin resistance.Semantic proximity Read ↗

Single and dual mutations at positions 2058, 2503 and 2504 of 23S rRNA and their relationship to resistance to antibiotics that target the large ribosomal subunit.Semantic proximity Read ↗

Mutations in 23S rRNA at the peptidyl transferase center and their relationship to linezolid binding and cross-resistance.Semantic proximity Read ↗

Analysis of mutations at residues A2451 and G2447 of 23S rRNA in the peptidyltransferase active site of the 50S ribosomal subunit.Semantic proximity Read ↗

A ketolide resistance mutation in domain II of 23S rRNA reveals the proximity of hairpin 35 to the peptidyl transferase centre.Semantic proximity Read ↗

Chemical engineering of the peptidyl transferase center reveals an important role of the 2'-hydroxyl group of A2451.Semantic proximity Read ↗

Mutations in the conserved P loop perturb the conformation of two structural elements in the peptidyl transferase center of 23 S ribosomal RNA.Semantic proximity Read ↗

Base-pairing between 23S rRNA and tRNA in the ribosomal A site.Semantic proximity Read ↗

Mutagenesis of the peptidyltransferase center of 23S rRNA: the invariant U2449 is dispensable.Semantic proximity Read ↗

Selection for intragenic suppressors of lethal 23S rRNA mutations in Escherichia coli identifies residues important for ribosome assembly and function.Semantic proximity Read ↗

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