The DOI matches its Crossref record; 46 of the 46 references it cites were found in a registry or an index.
Sequence selectivity of macrolide-induced translational attenuation
Open accessAbstract
Significance: By globally mapping the position of stalled ribosomes in macrolide-treated Staphylococcus aureus , we identified the proteins whose synthesis is affected by this antibiotic. Rather than acting as a nonselective inhibitor, the binding of macrolides to the ribosome tunnel only induces stalling at a few unique sites that are enriched in proline and charged residues. The sequences that flank the stalling sites are highly variable but are essential for efficient stalling. Although it has long been assumed that macrolides inhibit translation after the synthesis of a few residues, we found that stalling could occur at any point during translation. Our results reveal a striking conservation of stalling motifs among all known arrest peptides that strongly suggests a universal ribosome stalling mechanism.
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“Recent studies on NPET binding translation inhibitors like macrolides and Tetracenomycin X have established that the sequence of the nascent peptide plays a crucial role in the binding affinity and efficacy of these inhibitors14,26,27.”
From Dual site targeting of the bacterial 70S ribosome by tetracyclines (2026) · cites this paper as [26]
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Genome-Wide Analysis in Vivo of Translation with Nucleotide Resolution Using Ribosome Profiling
Ingolia, N. T., Ghaemmaghami, S., Newman, J. R. S., & Weissman, J. S. (2009) · Science · doi:10.1126/science.1168978 · Cited by 3,853
The Structural Basis of Ribosome Activity in Peptide Bond Synthesis
Nissen, P., Hansen, J., Ban, N., Moore, P. B., & Steitz, T. A. (2000) · Science · doi:10.1126/science.289.5481.920 · Cited by 2,269
The world of subinhibitory antibiotic concentrations
DAVIES, J. E., Spiegelman, G. B., & Yim, G. (2006) · Current Opinion in Microbiology · doi:10.1016/j.mib.2006.08.006 · Cited by 740
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The anti-Shine–Dalgarno sequence drives translational pausing and codon choice in bacteria
Li, G., Oh, E., & Weissman, J. S. (2012) · Nature · doi:10.1038/nature10965 · Cited by 644
eIF5A Promotes Translation of Polyproline Motifs
Gutierrez, E., Shin, B., Woolstenhulme, C. J., Kim, J.-R., Saini, P., Buskirk, A. R., & Dever, T. E. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.04.021 · Cited by 544
The Ribosomal Exit Tunnel Functions as a Discriminating Gate
Nakatogawa, H., & Ito, K. (2002) · Cell · doi:10.1016/s0092-8674(02)00649-9 · Cited by 533
EF-P Is Essential for Rapid Synthesis of Proteins Containing Consecutive Proline Residues
Doerfel, L. K., Wohlgemuth, I., Kothe, C., Peske, F., Urlaub, H., & Rodnina, M. V. (2012) · Science · doi:10.1126/science.1229017 · Cited by 490
Selective Ribosome Profiling Reveals the Cotranslational Chaperone Action of Trigger Factor In Vivo
Oh, E., Becker, A. H., Sandikci, A., Huber, D., Chaba, R., Gloge, F., Nichols, R. J., Typas, A., Gross, C. A., Krämer, G., et al. (2011) · Cell · doi:10.1016/j.cell.2011.10.044 · Cited by 468
Tenson, T., Lovmar, M., & Ehrenberg, M. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00662-4 · Cited by 461
Cited by
Sorted by citations
Ribosome profiling reveals the what, when, where and how of protein synthesis
Brar, G. A., & Weissman, J. S. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm4069 · Cited by 559
The macrolide antibiotic renaissance
Dinos, G. P. (2017) · British Journal of Pharmacology · doi:10.1111/bph.13936 · Cited by 512
How Macrolide Antibiotics Work
Vázquez‐Laslop, N., & Mankin, A. S. (2018) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2018.06.011 · Cited by 460
Lin, J., Zhou, D., Steitz, T. A., Polikanov, Y. S., & Gagnon, M. G. (2018) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-062917-011942 · Cited by 414
Genome-wide Survey of Ribosome Collision
Han, P., Shichino, Y., Schneider‐Poetsch, T., Mito, M., Hashimoto, S., Udagawa, T., Kohno, K., Yoshida, M., Mishima, Y., Inada, T., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107610 · Cited by 183
Metadata
- Authors
- Davis, A. R., Gohara, D. W., & Yap, M.-N. F.
- Affiliations
- Saint Louis University (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2014-10-13
- Volume
- 111
- Issue
- 43
- Pages
- 15379-15384
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC4217412
- OpenAlex
- W2165035045
- Cited by
- 123
- References
- 46
- Citations by year
- 2026: 13 · 2025: 10 · 2024: 10 · 2023: 6 · 2022: 8 · 2021: 14 · 2020: 12 · 2019: 8 · 2018: 11 · 2017: 18 · 2016: 10 · 2015: 3
- FWCI
- 4.23
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Saint Louis University
- National Institutes of Health
- National Institute of General Medical Sciences (R00GM094212)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Immunology and Microbiology › Applied Microbiology and Biotechnology › Microbial Natural Products and Biosynthesis
- Keywords
- macrolide antibiotics, azithromycin, translational attenuation, ribosome stalling, Staphylococcus aureus, proline-rich sequences, charged residues, translational arrest
- MeSH terms
- Peptides, Proline, Ribosomes, Staphylococcus aureus, Protein Biosynthesis, Open Reading Frames, Azithromycin, Macrolides, Sequence Analysis, Protein
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