Journal of Molecular Biology
CommunicationMutations in Domain II of 23 S rRNA Facilitate Translation of a 23 S rRNA-encoded Pentapeptide Conferring Erythromycin Resistance
References (0)
Cited by (33)
The ribosome as a missing link in prebiotic evolution II: Ribosomes encode ribosomal proteins that bind to common regions of their own mRNAs and rRNAs
2016, Journal of Theoretical BiologyCitation Excerpt :In recent years, exploration of open reading frames in both prokaryotes and eukaryotes has, however, yielded the surprising observation that some of their rRNA and rDNA sequences can be translated into peptides and proteins that have functional activity. For example, Tenson and Mankin (1995), Tenson et al. (1996) and Dam et al. (1996) have demonstrated in various bacteria that there is a, “short open reading frame in the 23S rRNA that encodes a pentapeptide (E-peptide) whose expression in vivo renders cells resistant to erythromycin.” Tenson and Mankin (1995) and Tenson et al. (1996) have shown that this peptide binds directly to the 23S rRNA, exerting its function through this interaction.
Macrolide resistance in Streptococci and Haemophilus influenzae
2004, Clinics in Laboratory MedicineMode of Action and Resistance Mechanisms of Antimicrobial Macrolides
2003, Macrolide Antibiotics: Chemistry, Biology, and Practice: Second EditionMolecular basis of clarithromycin-resistance in Mycobacterium avium intracellulare complex
2000, Tubercle and Lung Disease
- f1
Permanent address: T. Tenson, Institute of Molecular and Cellular Biology, Tartu University, Tartu, Estonia.
- f2
Corresponding author