ArticleJournal of bacteriology1994
Ribosomal protein gene sequence changes in erythromycin-resistant mutants of Escherichia coli.
Article in Journal of bacteriology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
61 citing papers in PubMed, 136 citations in OpenAlex.
- Genetic basis of clarithromycin resistance inMicrobiology spectrum · 2024Article
- Mitochondrial genome diversity ofFrontiers in microbiology · 2023Article
- Variability ofAntibiotics (Basel, Switzerland) · 2022Review
- Ψ-Footprinting approach for the identification of protein synthesis inhibitor producers.NAR genomics and bioinformatics · 2022Article
- Multiple Mechanisms Confer Resistance to Azithromycin inMicrobiology spectrum · 2022Article
- A Survey of Spontaneous Antibiotic-Resistant Mutants of the Halophilic, Thermophilic BacteriumAntibiotics (Basel, Switzerland) · 2021Article
- DNA Breaks-Mediated Fitness Cost Reveals RNase HI as a New Target for Selectively Eliminating Antibiotic-Resistant Bacteria.Molecular biology and evolution · 2021Article
- Mutational Activation of Antibiotic-Resistant Mechanisms in the Absence of Major Drug Efflux Systems of Escherichia coli.Journal of bacteriology · 2021Article
- Antimicrobial Resistance Determinants Circulating among ThermophilicAntibiotics (Basel, Switzerland) · 2020Article
- Antibiotic susceptibility of plant-derived lactic acid bacteria conferring health benefits to human.The Journal of antibiotics · 2019Article
- Structure of Dirithromycin Bound to the Bacterial Ribosome Suggests New Ways for Rational Improvement of Macrolides.Antimicrobial agents and chemotherapy · 2019Article
- Increased freedom of movement in the nascent chain results in dynamic changes in the structure of the SecM arrest motif.Bioscience reports · 2019Article
- Twenty-seven-nucleotide repeat insertion in theOncotarget · 2018Article
- An antimicrobial peptide that inhibits translation by trapping release factors on the ribosome.Nature structural & molecular biology · 2017Article
- The extended loops of ribosomal proteins uL4 and uL22 of Escherichia coli contribute to ribosome assembly and protein translation.Nucleic acids research · 2016Article
- A global map of genetic diversity in Babesia microti reveals strong population structure and identifies variants associated with clinical relapse.Nature microbiology · 2016Article
- Targeting Antibiotic Resistance.Angewandte Chemie (International ed. in English) · 2016Review
- Macrolide Resistance inFrontiers in cellular and infection microbiology · 2016Review
- tRNAs as antibiotic targets.International journal of molecular sciences · 2014Review
- Regional discrimination and propagation of local rearrangements along the ribosomal exit tunnel.Journal of molecular biology · 2014Article
1 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The genes for ribosomal proteins L4 and L22 from two erythromycin-resistant mutants of Escherichia coli have been isolated and sequenced. In the L4 mutant, an A-to-G transition in codon 63 predicted a Lys-to-Glu change in the protein. In the L22 strain, a 9-bp deletion removed codons 82 to 84, eliminating the sequence Met-Lys-Arg from the protein. Consistent with these DNA changes, in comparison with wild-type proteins, both mutant proteins had reduced first-dimension mobilities in two-dimensional polyacrylamide gels. Complementation of each mutation by a wild-type gene on a plasmid vector resulted in increased erythromycin sensitivity in the partial-diploid strains. The fraction of ribosomes containing the mutant form of the protein was increased by growth in the presence of erythromycin. Erythromycin binding was increased by the fraction of wild-type protein present in the ribosome population. The strain with the L4 mutation was found to be cold sensitive for growth at 20 degrees C, and 50S-subunit assembly was impaired at this temperature. The mutated sequences are highly conserved in the corresponding proteins from a number of species. The results indicate the participation of these proteins in the interaction of erythromycin with the ribosome.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.