Mutation from guanine to adenine in 25S rRNA at the position equivalent to E. coli A2058 does not confer erythromycin sensitivity in Sacchromyces cerevisae
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Date
2008-03
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Citation of Original Publication
Ananth S. Bommakanti , et.al, Mutation from guanine to adenine in 25S rRNA at the position equivalent to E. coli A2058 does not confer erythromycin sensitivity in Sacchromyces cerevisae, RNA. 2008 Mar; 14(3): 460–464. DOI: 10.1261/rna.786408
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Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)
Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)
Subjects
ribosome
macrolide
peptidyltransferase
peptide exit tunnel
macrolide
peptidyltransferase
peptide exit tunnel
Abstract
The macrolide erythromycin binds to the large subunit of the prokaryotic ribosome near the peptidyltransferase center (PTC)
and inhibits elongation of new peptide chains beyond a few amino acids. Nucleotides A2058 and A2059 (E. coli numbering) in
23S rRNA play a crucial role in the binding of erythromycin, and mutation of nucleotide A2058 confers erythromycin resistance
in both Gram-positive and Gram-negative bacteria. There are high levels of sequence and structural similarity in the PTC of
prokaryotic and eukaryotic ribosomes. However, eukaryotic ribosomes are resistant to erythromycin and the presence of a G at
the position equivalent to E. coli nucleotide A2058 is believed to be the reason. To test this hypothesis, we introduced a G to
A mutation at this position of the yeast Saccharomyces cerevisiae 25S rRNA and analyzed sensitivity toward erythromycin.
Neither growth studies nor erythromycin binding assays on mutated yeast ribosomes indicated any erythromycin sensitivity in
mutated yeast strains. These results suggest that the identity of nucleotide 2058 is not the only determinant responsible for the
difference in erythromycin sensitivity between yeast and prokaryotes.