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Structure of the 70 S Ribosome Complexed with mRNA and tRNA
Abstract
The crystal structure of the bacterial 70 S ribosome refined to 2.8 angstrom resolution reveals atomic details of its interactions with messenger RNA (mRNA) and transfer RNA (tRNA). A metal ion stabilizes a kink in the mRNA that demarcates the boundary between A and P sites, which is potentially important to prevent slippage of mRNA. Metal ions also stabilize the intersubunit interface. The interactions of E-site tRNA with the 50 S subunit have both similarities and differences compared to those in the archaeal ribosome. The structure also rationalizes much biochemical and genetic data on translation.
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Citations
Cites
Crystal structure of the ribosome at 5.5 Å resolution
Yusupov, M. M., Yusupova, G. Z., Baucom, A., Lieberman, K., Earnest, T. N., Cate, J. H. D., & Noller, H. F. (2001) · Science · doi:10.1126/science.1060089 · Cited by 1,944
Geigenmüller, U., & Nierhaus, K. H. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07904.x · Cited by 68
Cited by
RELION: Implementation of a Bayesian approach to cryo-EM structure determination
Scheres, S. H. W. (2012) · Journal of Structural Biology · doi:10.1016/j.jsb.2012.09.006 · Cited by 5,446
Regulation of Translation Initiation in Eukaryotes: Mechanisms and Biological Targets
Sonenberg, N., & Hinnebusch, A. G. (2009) · Cell · doi:10.1016/j.cell.2009.01.042 · Cited by 3,304
“The stunning progress on crystal structures of bacterial 70S ribosomes bound to mRNAs and tRNAs (Selmer et al., 2006; Yusupova et al., 2006) has provided atomic details of the path of mRNA and contacts made with tRNAs in the decoding sites.”
The Spliceosome: Design Principles of a Dynamic RNP Machine
Wahl, M. C., Will, C. L., & Lührmann, R. (2009) · Cell · doi:10.1016/j.cell.2009.02.009 · Cited by 2,665
Burley, S. K., Bhikadiya, C., Bi, C., Bittrich, S., Chen, L., Crichlow, G. V., Christie, C. H., Dalenberg, K., Di Costanzo, L., Duarte, J. M., et al. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkaa1038 · Cited by 1,581
Ribosome-targeting antibiotics and mechanisms of bacterial resistance
Wilson, D. N. (2014) · Nature Reviews Microbiology · doi:10.1038/nrmicro3155 · Cited by 1,054
The Scanning Mechanism of Eukaryotic Translation Initiation
Hinnebusch, A. G. (2014) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060713-035802 · Cited by 798
Encoding multiple unnatural amino acids via evolution of a quadruplet-decoding ribosome
Neumann, H., Wang, K., Davis, L., Garcia-Alai, M., & Chin, J. W. (2010) · Nature · doi:10.1038/nature08817 · Cited by 622
The Structure of the Ribosome with Elongation Factor G Trapped in the Posttranslocational State
Gao, Y.-G., Selmer, M., Dunham, C. M., Weixlbaumer, A., Kelley, A. C., & Ramakrishnan, V. (2009) · Science · doi:10.1126/science.1179709 · Cited by 513
Self-citationOne core, two shells: bacterial and eukaryotic ribosomes
Melnikov, S., Ben-Shem, A., Garreau de Loubresse, N., Jenner, L., Yusupova, G., & Yusupov, M. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2313 · Cited by 477
Structure and Mechanism of a Metal-Sensing Regulatory RNA
Dann, C. E., Wakeman, C. A., Sieling, C. L., Baker, S. C., Irnov, I., & Winkler, W. C. (2007) · Cell · doi:10.1016/j.cell.2007.06.051 · Cited by 386
The Mechanism for Activation of GTP Hydrolysis on the Ribosome
Voorhees, R. M., Schmeing, T. M., Kelley, A. C., & Ramakrishnan, V. (2010) · Science · doi:10.1126/science.1194460 · Cited by 366
Self-citationToh, S., Xiong, L., Arias, C. A., Villegas, M. V., Lolans, K., Quinn, J., & Mankin, A. S. (2007) · Molecular Microbiology · doi:10.1111/j.1365-2958.2007.05744.x · Cited by 338
Structural aspects of messenger RNA reading frame maintenance by the ribosome
Jenner, L. B., Demeshkina, N., Yusupova, G., & Yusupov, M. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1790 · Cited by 312
The A-Z of bacterial translation inhibitors
Wilson, D. N. (2009) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409230903307311 · Cited by 322
Coupling of Ribosomal L1 Stalk and tRNA Dynamics during Translation Elongation
Fei, J., Kosuri, P., MacDougall, D. D., & Gonzalez, R. L. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.03.012 · Cited by 316
Revisiting the structures of several antibiotics bound to the bacterial ribosome
Bulkley, D., Innis, C. A., Blaha, G., & Steitz, T. A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1008685107 · Cited by 308
An integrated, structure- and energy-based view of the genetic code
Grosjean, H., & Westhof, E. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw608 · Cited by 278
Structure of the bacterial ribosome at 2 Å resolution
Watson, Z. L., Ward, F. R., Méheust, R., Ad, O., Schepartz, A., Banfield, J. F., & Cate, J. H. (2020) · eLife · doi:10.7554/elife.60482 · Cited by 263
Origin and evolution of the ribosome
Fox, G. E. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a003483 · Cited by 258
Wolf, Y. I., & Koonin, E. V. (2007) · Biology Direct · doi:10.1186/1745-6150-2-14 · Cited by 235
Crystal structures of EF-G-ribosome complexes trapped in intermediate states of translocation
Zhou, J., Lancaster, L., Donohue, J. P., & Noller, H. F. (2013) · Science · doi:10.1126/science.1236086 · Cited by 229
A hierarchical model for evolution of 23S ribosomal RNA
Bokov, K., & Steinberg, S. V. (2009) · Nature · doi:10.1038/nature07749 · Cited by 228
Gebetsberger, J., Wyss, L., Mleczko, A. M., Reuther, J., & Polacek, N. (2017) · RNA Biology · doi:10.1080/15476286.2016.1257470 · Cited by 222
Root of the Tree: The Significance, Evolution, and Origins of the Ribosome
Bowman, J. C., Petrov, A. S., Frenkel-Pinter, M., Penev, P. I., & Williams, L. D. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00742 · Cited by 197
Visualizing translation dynamics at atomic detail inside a bacterial cell
Xue, L., Lenz, S., Zimmermann-Kogadeeva, M., Tegunov, D., Cramer, P., Bork, P., Rappsilber, J., & Mahamid, J. (2022) · Nature · doi:10.1038/s41586-022-05255-2 · Cited by 184
Rozov, A., Khusainov, I., El Omari, K., Duman, R., Mykhaylyk, V., Yusupov, M., Westhof, E., Wagner, A., & Yusupova, G. (2019) · Nature Communications · doi:10.1038/s41467-019-10409-4 · Cited by 179
The Ribosomal Peptidyl Transferase
Beringer, M., & Rodnina, M. V. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.03.015 · Cited by 172
Evolution of Protein Synthesis from an RNA World
Noller, H. F. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a003681 · Cited by 155
SecM-Stalled Ribosomes Adopt an Altered Geometry at the Peptidyl Transferase Center
Bhushan, S., Hoffmann, T., Seidelt, B., Frauenfeld, J., Mielke, T., Berninghausen, O., Wilson, D. N., & Beckmann, R. (2011) · PLoS Biology · doi:10.1371/journal.pbio.1000581 · Cited by 154
Mechanism of tetracycline resistance by ribosomal protection protein Tet(O)
Li, W., Atkinson, G. C., Thakor, N. S., Allas, Ü., Lu, C.-C., Chan, K.-Y., Tenson, T., Schulten, K., Wilson, K. S., Hauryliuk, V., et al. (2013) · Nature Communications · doi:10.1038/ncomms2470 · Cited by 147
Preferred and avoided codon pairs in three domains of life
Tats, A., Tenson, T., & Remm, M. (2008) · BMC Genomics · doi:10.1186/1471-2164-9-463 · Cited by 112
“Unfortunately, we currently have very limited information about the details of interaction between different tRNAs with the ribosome [29,34,35], which precludes further extension of this hypothesis.”
BackgroundRibosome binding of a single copy of the SecY complex: implications for protein translocation.
Ménétret, J.-F., Schaletzky, J., Clemons, W. M., Osborne, A. R., Skånland, S. S., Denison, C., Gygi, S. P., Kirkpatrick, D. S., Park, E., Ludtke, S. J., et al. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.10.034 · Cited by 108
The Ribosome Challenge to the RNA World
Bowman, J. C., Hud, N. V., & Williams, L. D. (2015) · Journal of Molecular Evolution · doi:10.1007/s00239-015-9669-9 · Cited by 99
Bidentate RNA–magnesium clamps: On the origin of the special role of magnesium in RNA folding
Petrov, A. S., Bowman, J. C., Harvey, S. C., & Williams, L. D. (2011) · RNA · doi:10.1261/rna.2390311 · Cited by 94
Mutations outside the anisomycin-binding site can make ribosomes drug-resistant
Blaha, G., Gürel, G., Schroeder, S. J., Moore, P. B., & Steitz, T. A. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.03.075 · Cited by 88
Camprubí, E., de Leeuw, J. W., House, C. H., Raulin, F., Russell, M. J., Spang, A., Tirumalai, M. R., & Westall, F. (2019) · Space Science Reviews · doi:10.1007/s11214-019-0624-8 · Cited by 84
Imprints of the genetic code in the ribosome
Johnson, D. B. F., & Wang, L. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1000704107 · Cited by 83
Wasserman, M. R., Pulk, A., Zhou, Z., Altman, R. B., Zinder, J. C., Green, K. D., Garneau-Tsodikova, S., Doudna Cate, J. H., & Blanchard, S. C. (2015) · Nature Communications · doi:10.1038/ncomms8896 · Cited by 77
Ribosomal proteins: Structure, function, and evolution
Korobeinikova, A. V., Garber, M. B., & Gongadze, G. M. (2012) · Biochemistry (Moscow) · doi:10.1134/s0006297912060028 · Cited by 63
Multiple prebiotic metals mediate translation
Bray, M. S., Lenz, T. K., Haynes, J. W., Bowman, J. C., Petrov, A. S., Reddi, A. R., Hud, N. V., Williams, L. D., & Glass, J. B. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1803636115 · Cited by 58
The final step of 40S ribosomal subunit maturation is controlled by a dual key lock
Plassart, L., Shayan, R., Montellese, C., Rinaldi, D., Larburu, N., Pichereaux, C., Froment, C., Lebaron, S., O'Donohue, M.-F., Kutay, U., et al. (2021) · eLife · doi:10.7554/elife.61254 · Cited by 55
The Peptidyl Transferase Center: a Window to the Past
Tirumalai, M. R., Rivas, M., Tran, Q., & Fox, G. E. (2021) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00104-21 · Cited by 53
Nucleotide modifications and tRNA anticodon–mRNA codon interactions on the ribosome
Allnér, O., & Nilsson, L. (2011) · RNA · doi:10.1261/rna.029231.111 · Cited by 50
Modulating co-translational protein folding by rational design and ribosome engineering
Ahn, M., Włodarski, T., Mitropoulou, A., Chan, S. H. S., Sidhu, H., Plessa, E., Becker, T. A., Budisa, N., Waudby, C. A., Beckmann, R., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31906-z · Cited by 45
Molecular paleontology: a biochemical model of the ancestral ribosome
Hsiao, C., Lenz, T. K., Peters, J. K., Fang, P.-Y., Schneider, D. M., Anderson, E. J., Preeprem, T., Bowman, J. C., O'Neill, E. B., Lie, L., et al. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt023 · Cited by 45
Lawrence, M. G., Shamsuzzaman, M., Kondopaka, M., Pascual, C., Zengel, J. M., & Lindahl, L. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw493 · Cited by 36
Diverse relationships between metal ions and the ribosome
Akanuma, G. (2021) · Bioscience, Biotechnology, and Biochemistry · doi:10.1093/bbb/zbab070 · Cited by 34
Arora, S., Bhamidimarri, S. P., Bhattacharyya, M., Govindan, A., Weber, M. H. W., Vishveshwara, S., & Varshney, U. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt175 · Cited by 33
Mutagenesis of the modified bases, m5U1939 and ψ2504, in Escherichia coli 23S rRNA
Persaud, C., Lu, Y., Vila-Sanjurjo, A., Campbell, J. L., Finley, J., & O’Connor, M. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.01.021 · Cited by 33
The Ribosome: Some Hard Facts about Its Structure and Hot Air about Its Evolution
Ramakrishnan, V. (2009) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2009.74.032 · Cited by 27
Self-citationLomakin, I. B., Devarkar, S. C., Patel, S., Grada, A., & Bunick, C. G. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad103 · Cited by 25
Kumar, N., Sharma, S., & Kaushal, P. S. (2024) · Nature Communications · doi:10.1038/s41467-024-44879-y · Cited by 20
Origins and Early Evolution of the Ribosome
Fox, G. E. (2016) · Evolution of the Protein Synthesis Machinery and Its Regulation · doi:10.1007/978-3-319-39468-8_3 · Cited by 10
Structural insights into context-specific inhibition of bacterial translation by macrolides
Syroegin, E. A., Aleksandrova, E. V., Kruglov, A. A., Paranjpe, M. N., Svetlov, M. S., & Polikanov, Y. S. (2025) · Nature Communications · doi:10.1038/s41467-025-64692-5 · Cited by 8
Metadata
- Authors
- Selmer, M., Dunham, C. M., Murphy, F. V., Weixlbaumer, A., Petry, S., Kelley, A. C., Weir, J. R., & Ramakrishnan, V.
- Venue
- Science
- Published
- 2006-09-29
- Volume
- 313
- Issue
- 5795
- Pages
- 1935-1942
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2022754910
- Cited by
- 1,283
- References
- 2
- FWCI
- 45.19
- Type
- journal article
- Language
- en
- Open access
- closed
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