Crystal structures of complexes of the small ribosomal subunit with tetracycline, edeine and IF3
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The small ribosomal subunit is responsible for the decoding of genetic information and plays a key role in the initiation of protein synthesis. We analyzed by X-ray crystallography the structures of three different complexes of the small ribosomal subunit of Thermus thermophilus with the A-site inhibitor tetracycline, the universal initiation inhibitor edeine and the C-terminal domain of the translation initiation factor IF3. The crystal structure analysis of the complex with tetracycline revealed the functionally important site responsible for the blockage of the A-site. Five additional tetracycline sites resolve most of the controversial biochemical data on the location of tetracycline. The interaction of edeine with the small subunit indicates its role in inhibiting initiation and shows its involvement with P-site tRNA. The location of the C-terminal domain of IF3, at the solvent side of the platform, sheds light on the formation of the initiation complex, and implies that the anti-association activity of IF3 is due to its influence on the conformational dynamics of the small ribosomal subunit.
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Tetracycline binding at the second site has not been previously described.
“Tetracycline binding at this position has not been previously described (17 -20).”
From Resistance mutations generate divergent antibiotic susceptibility profiles against translation inhibitors (2016) · cites this paper as [17]
Negamycin and tetracycline possess chemically distinct features that form different sets of electrostatic and van der Waals interactions, specifically with h31 and h34.
“Despite the overlapping binding sites, negamycin and tetracycline possess chemically distinct features (Fig. 2 B ) that form different sets of electrostatic and van der Waals interactions, specifically with h31 and h34 (11, 12, 17).”
From Resistance mutations generate divergent antibiotic susceptibility profiles against translation inhibitors (2016) · cites this paper as [17]
The Tet-1 and primary tetracycline binding sites are located in the ribosomal A site, bound by the irregular minor groove of helix 34 and the loop of helix 31 in 16S rRNA.
“In this respect, the Tet-1 and primary site in the Pioletti and Brodersen structures, respectively (Fig. 2), are located in the ribosomal A site, where tetracycline is bound by the irregular minor groove of helix 34 (h34) and the loop of helix 31 (h31) in the 16S rRNA (4, 37).”
From Ribosomal Protection Proteins and Their Mechanism ofTetracyclineResistance (2003) · cites this paper as [37]
The secondary and Tet-5 tetracycline-binding sites are likely candidates for the inhibitory binding site.
“The secondary and Tet-5 tetracycline-binding sites (Fig. 2) are also likely candidates for the inhibitory binding site (4, 37).”
From Ribosomal Protection Proteins and Their Mechanism ofTetracyclineResistance (2003) · cites this paper as [37]
The primary (and Tet-1) site is the most highly occupied site in both structures showing tetracycline bound to the 30S subunit, consistent with the high-affinity site being the inhibitory site.
“(i) the primary (and Tet-1) site is the most highly occupied site in both structures showing tetracycline bound to the 30S subunit (4, 37) consistent with the idea that the high-affinity site is the inhibitory site (17, 47, 56).”
From Ribosomal Protection Proteins and Their Mechanism ofTetracyclineResistance (2003) · cites this paper as [37]
Two independent 30S subunit-tetracycline crystal structures show tetracycline bound to either two or six sites on the 30S ribosomal subunit.
“This is significant, as two independent 30S subunit-tetracycline crystal structures show tetracycline bound to either two (4) or six sites (37) on the 30S ribosomal subunit (Fig. 2).”
From Ribosomal Protection Proteins and Their Mechanism ofTetracyclineResistance (2003) · cites this paper as [37]
In the primary/Tet-1 position, tetracycline is believed to sterically interfere with aa-tRNA binding.
“In this position, it is believed that tetracycline would sterically interfere with aa-tRNA binding (4, 37).”
From Ribosomal Protection Proteins and Their Mechanism ofTetracyclineResistance (2003) · cites this paper as [37]
Differences in domain IV may serve to distinguish Tet(O) and EF-G with respect to their activities; domain IV of EF-G more intimately overlaps with the A site-bound tRNA, consistent with its role in translocation, whereas interaction of domain IV of Tet(O) and h34 of the 30S subunit is consistent with its role in tetracycline release because h34 is a component of the primary tetracycline binding.
“In this case, these differences in domain IV may serve to distinguish Tet(O) and EF-G with respect to their activities; namely, domain IV of EF-G more intimately overlaps with the A site-bound tRNA, an idea that is consistent with the role of domain IV of EF-G in translocation. In contrast, the interaction of domain IV of Tet(O) and h34 of the 30S subunit is consistent with its role in tetracycl”
From Ribosomal Protection Proteins and Their Mechanism ofTetracyclineResistance (2003) · cites this paper as [37]
The proposed conformational change resulting in tetracycline release probably involves h34.
“The proposed conformational change resulting in tetracycline release probably involves h34 as (i) h34 forms an integral part of the primary tetracycline binding site (4, 37), (ii) cryo-EM reconstructions show that domain IV of Tet(O) contacts the base of h34 (45), and (iii) Tet(O) protects C1214 at the base of h34 from chemical modification by DMS (12).”
From Ribosomal Protection Proteins and Their Mechanism ofTetracyclineResistance (2003) · cites this paper as [37]
Tet(O) invokes structural rearrangements in h44.
“In addition to the proposed conformational change in h34 that results in tetracycline release, Tet(O) invokes structural rearrangements in h44 (12), a site distinct from both the primary tetracycline binding site (4, 37) and the Tet(O) binding site observed in the cryo-EM reconstruction (45).”
From Ribosomal Protection Proteins and Their Mechanism ofTetracyclineResistance (2003) · cites this paper as [37]
A gross conformational change is not observed in the crystal structure of tetracycline bound to the 30S subunit.
“Although a gross conformational change is not observed in the crystal structure of tetracycline bound to the 30S subunit (4, 37)”
From Ribosomal Protection Proteins and Their Mechanism ofTetracyclineResistance (2003) · cites this paper as [37]
Additional density in the TetM•70S map fuses directly with C1054 of the 16S rRNA, a component of the primary tetracycline binding site.
“This additional density in the TetM•70S map fuses directly with C1054 of the 16S rRNA, a component of the primary tetracycline binding site (2, 3), and is consistent with the protection of C1054 from DMS modification observed upon TetO binding to the ribosome (15).”
From Structural basis for TetM-mediated tetracycline resistance (2012) · cites this paper as [3]
No additional density for tigecycline is observed within any of the secondary tetracycline binding sites in the TetM•70S map.
“In contrast to tetracycline, which has multiple binding sites on the ribosome (2, 3), a careful examination of the TetM•70S map reveals no additional density for Tgc within any of the sec- ondary tetracycline binding sites (SI Appendix, Fig. S10 I-M).”
From Structural basis for TetM-mediated tetracycline resistance (2012) · cites this paper as [3]
Crystal structures of the 30S ribosomal subunit in complex with tetracycline reveal the primary binding site to be located in helix 34 of the 16S rRNA, in a position overlapping with the anticodon stem-loop of A-site tRNA.
“Consistently, crystal structures of the small (30S) ribosomal subunit in complex with tetracycline reveal the primary binding site to be located in helix 34 (h34) of the 16S rRNA, in a position overlapping with the anticodon stem-loop of A-site tRNA (A-tRNA) (2, 3).”
From Structural basis for TetM-mediated tetracycline resistance (2012) · cites this paper as [3]
The observed binding position of tigecycline was modeled into the primary tetracycline binding site based on similarity of the chemical structures of tigecycline and tetracycline.
“Because there is no structure reported for Tgc•70S, the observed binding position of Tgc was modeled into the primary tetracycline binding site (2, 3) based on similarity of the chemical structures of the two drugs (SI Appendix, Fig. S10 D-H).”
From Structural basis for TetM-mediated tetracycline resistance (2012) · cites this paper as [3]
Tetracycline antibiotics bind to the bacterial 30S ribosomal subunit and prevent chain elongation by blocking aminoacyl-tRNA binding to the A site.
“Tetracycline antibiotics bind to the bacterial 30S ribosomal subunit and prevent chain elongation by blocking aminoacyl-tRNA binding to the A site (3, 21, 27).”
From Target- and resistance-based mechanistic studies with TP-434, a novel fluorocycline antibiotic (2012) · cites this paper as [27]
Both 30S ribosome crystal structures include four residues of the h31 loop, 964 to 967, in the primary or Tet-1 binding site.
“As mentioned, both 30S ribosome crystal structures include four residues of the h31 loop, 964 to 967, in the primary or Tet-1 binding site (4, 23).”
From Mutations in the 16S rRNA Genes of<i>Helicobacter pylori</i>Mediate Resistance to Tetracycline (2002) · cites this paper as [23]
The occupancy of the Tet-4 site by tetracycline in the 30S subunit-tetracycline crystal structure is only half of that of the Tet-1 site.
“The occupancy of the Tet-4 site by tetracycline in the 30S subunit-tetracycline crystal structure is only half of that of the Tet-1 site (23).”
From Mutations in the 16S rRNA Genes of<i>Helicobacter pylori</i>Mediate Resistance to Tetracycline (2002) · cites this paper as [23]
The residue identified in tetracycline-resistant P. acnes mutants is directly adjacent to the primary binding site, but this mutation did not mediate tetracycline resistance in H. pylori.
“The residue identified in the tetracycline-resistant P. acnes mutants is directly adjacent to the primary binding site (4, 23, 25), but this mutation did not mediate tetracycline resistance in H. pylori.”
From Mutations in the 16S rRNA Genes of<i>Helicobacter pylori</i>Mediate Resistance to Tetracycline (2002) · cites this paper as [23]
The G942 residue is located at the Tet-4 binding site identified in one of the 30S structures and is deleted in strain 109.
“This residue is located at the Tet-4 binding site identified in one of the 30S structures (23) and is deleted in strain 109.”
From Mutations in the 16S rRNA Genes of<i>Helicobacter pylori</i>Mediate Resistance to Tetracycline (2002) · cites this paper as [23]
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Cites
[20] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475 · see citing works
Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse‐Kunstleve, R. W., Jiang, J., Kuszewski, J. J., Nilges, M., Pannu, N., et al. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998003254 · Cited by 15,720 · see citing works
Escherichia Coli and Salmonella: Typhimurium Cellular and Molecular Biology
Neidhardt, F. C., & Ingraham, J. L. (1987) · Medical Entomology and Zoology · Cited by 4,089 · see citing works
The Complete Atomic Structure of the Large Ribosomal Subunit at 2.4 Å Resolution
Ban, N., Nissen, P., Hansen, J., Moore, P. B., & Steitz, T. A. (2000) · Science · doi:10.1126/science.289.5481.905 · Cited by 3,327 · see citing works
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 · see citing works
Structure of the 30S ribosomal subunit
Wimberly, B. T., Brodersen, D. E., Clemons, W. M., Morgan-Warren, R. J., Carter, A. P., Vonrhein, C., Hartsch, T., & Ramakrishnan, V. (2000) · Nature · doi:10.1038/35030006 · Cited by 2,035 · see citing works
Self-citationCarter, A. P., Clemons, W. M., Brodersen, D. E., Morgan-Warren, R. J., Wimberly, B. T., & Ramakrishnan, V. (2000) · Nature · doi:10.1038/35030019 · Cited by 1,615 · see citing works
Molecular mechanisms that confer antibacterial drug resistance
Walsh, C. T. (2000) · Nature · doi:10.1038/35021219 · Cited by 1,579 · see citing works
Interaction of antibiotics with functional sites in 16S ribosomal RNA
Moazed, D., & Noller, H. F. (1987) · Nature · doi:10.1038/327389a0 · Cited by 1,150 · see citing works
Structure of Functionally Activated Small Ribosomal Subunit at 3.3 Å Resolution
Schluenzen, F., Tocilj, A., Zarivach, R., Harms, J., Gluehmann, M., Janell, D., Bashan, A., Bartels, H., Agmon, I., Franceschi, F., et al. (2000) · Cell · doi:10.1016/s0092-8674(00)00084-2 · Cited by 979 · see citing works
Self-citationBrodersen, D. E., Clemons, W. M., Carter, A. P., Morgan-Warren, R. J., Wimberly, B. T., & Ramakrishnan, V. (2000) · Cell · doi:10.1016/s0092-8674(00)00216-6 · Cited by 950 · see citing works
Fourmy, D., Recht, M. I., Blanchard, S. C., & Puglisi, J. D. (1996) · Science · doi:10.1126/science.274.5291.1367 · Cited by 829 · see citing works
Roberts, M. C. (1996) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.1996.tb00251.x · Cited by 689 · see citing works
X-ray Crystal Structures of 70 S Ribosome Functional Complexes
Cate, J. H. D., Yusupov, M., Yusupova, G. Z., Earnest, T. N., & Noller, H. F. (1999) · Science · doi:10.1126/science.285.5436.2095 · Cited by 583 · see citing works
Initiation of mRNA translation in prokaryotes
Gualerzi, C. O., & Pon, C. L. (1990) · Biochemistry · doi:10.1021/bi00477a001 · Cited by 502 · see citing works
Assembly Mapping of 30 S Ribosomal Proteins from Escherichia coli
Held, W. A., Ballou, B. T., Mizushima, S., & Nomura, M. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42644-6 · Cited by 425 · see citing works
Structure of Functionally Activated Small Ribosomal Subunit
Schluenzen, F., Tocilj, A., Zarivach, R., et al. (2000) · Cited by 331 · see citing works
Self-citationInteraction of antibiotics with A- and P-site-specific bases in 16S ribosomal RNA
Woodcock, J., Moazed, D., Cannon, M., Davies, J., & Noller, H. F. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07863.x · Cited by 229 · see citing works
Lodmell, J. S., & Dahlberg, A. E. (1997) · Science · doi:10.1126/science.277.5330.1262 · Cited by 212 · see citing works
Migration of 40 S ribosomal subunits on messenger RNA in the presence of edeine.
Kozak, M., & Shatkin, A. J. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)46969-x · Cited by 202 · see citing works
16S rRNA Mutation Associated with Tetracycline Resistance in a Gram-Positive Bacterium
Ross, J. I., Eady, E. A., Cove, J. H., & Cunliffe, W. J. (1998) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.42.7.1702 · Cited by 194 · see citing works
Godefroy-Colburn, T., Wolfe, A. D., DONDON, J., GRUNBERG‐MANAGO, M., Dessen, P., & Pantaloni, D. (1975) · Journal of Molecular Biology · doi:10.1016/0022-2836(75)90215-6 · Cited by 194 · see citing works
Carson, M. (1997) · PubMed · Cited by 178 · see citing works
Throwing a spanner in the works: antibiotics and the translation apparatus
Spahn, C. M. T., & Prescott, C. D. (1996) · Journal of Molecular Medicine · doi:10.1007/bf00217518 · Cited by 175 · see citing works
Throwing a spanner in the works: antibiotics and the translation apparatus
Spahn, C. M. T., & Prescott, C. D. (1996) · Journal of Molecular Medicine · doi:10.1007/s001090050044 · Cited by 154 · see citing works
Biou, V., Shu, F., & Ramakrishnan, V. (1995) · EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00077.x · Cited by 152 · see citing works
Location of translational initiation factor IF3 on the small ribosomal subunit
McCutcheon, J. P., Agrawal, R. K., Philips, S. M., et al. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.8.4301 · Cited by 151 · see citing works
Gordon, J. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63613-0 · Cited by 146 · see citing works
Mueller, F., & Brimacombe, R. L. C. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1210 · Cited by 136 · see citing works
Goldman, R. A., Hasan, T., Hall, C. C., Strycharz, W. A., & Cooperman, B. S. (1983) · Biochemistry · doi:10.1021/bi00271a020 · Cited by 134 · see citing works
O'Connor, M. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.6.1185 · Cited by 129 · see citing works
Nowotny, V., & Nierhaus, K. H. (1988) · Biochemistry · doi:10.1021/bi00418a057 · Cited by 123 · see citing works
Tocilj, A., Schlünzen, F., Janell, D., Gluehmann, M., Hansen, H. A. S., Harms, J., Bashan, A., Bartels, H., Agmon, I., Franceschi, F. J., et al. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.25.14252 · Cited by 118 · see citing works
Self-citationВладимирович, С. П., Lavrik, I. N., Wlasoff, V. A., Dokudovskaya, S., Dontsova, O. А., Bogdanov, A. A., & Brimacombe, R. L. C. (1997) · Europe PMC (PubMed Central) · Cited by 91 · see citing works
Tapprich, W. E., Goss, D. J., & Dahĺberg, A. E. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.13.4927 · Cited by 91 · see citing works
Translation initiation factor 3 antagonizes authentic start codon selection on leaderless mRNAs
Tedin, K., Moll, I., Grill, S., Resch, A., Graschopf, A., Gualerzi, C. O., & Bläsi, U. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01147.x · Cited by 91 · see citing works
Movement of the Decoding Region of the 16 S Ribosomal RNA Accompanies tRNA Translocation
VanLoock, M. S., Agrawal, R. K., Gabashvili, I. S., Qi, L., Frank, J., & Harvey, S. C. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.4213 · Cited by 85 · see citing works
Odon, O. W., Kramer, G., Henderson, A. B., et al. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)62324-0 · Cited by 77 · see citing works
Ehresmann, C., Moine, H., Mougel, M., et al. (1986) · Nucleic Acids Research · doi:10.1093/nar/14.12.4803 · Cited by 74 · see citing works
Gabashvili, I. S., Agrawal, R. K., Grassucci, R. A., Squires, C. L., Dahĺberg, A. E., & Frank, J. (1999) · The EMBO Journal · doi:10.1093/emboj/18.22.6501 · Cited by 73 · see citing works
Srivastava, S., Verschoor, A., & Frank, J. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90946-h · Cited by 72 · see citing works
Garcı́a, C., Fortier, P.-L., Blanquet, S., et al. (1995) · Journal of Molecular Biology · doi:10.1006/jmbi.1995.0615 · Cited by 72 · see citing works
Interaction of tetracycline with RNA: photoincorporation into ribosomal RNA of Escherichia coli
Oehler, R. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.6.1219 · Cited by 66 · see citing works
Tetracycline-Chelated Mg2+ Ion Initiates Helix Unwinding in Tet Repressor Induction,
Orth, P., Saenger, W., & Hinrichs, W. (1998) · Biochemistry · doi:10.1021/bi9816610 · Cited by 63 · see citing works
Gabashvili, I. S., Agrawal, R. K., Grassucci, R. A., & Frank, J. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.2538 · Cited by 60 · see citing works
Involvement of bases 787-795 of Escherichia coli 16S ribosomal RNA in ribosomal subunit association.
Tapprich, W. E., & Hill, W. E. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.3.556 · Cited by 55 · see citing works
Meinnel, T., Sacerdot, C., Graffe, M., et al. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.2881 · Cited by 55 · see citing works
Demeshkina, N., Repkova, M. N., Venyaminova, A. G., et al. (2000) · RNA · doi:10.1017/s1355838200000996 · Cited by 53 · see citing works
Moreau, M., Cock, E. D., Fortier, P.-L., et al. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0756 · Cited by 52 · see citing works
Genetic probes of ribosomal RNA function
O'Connor, M., Brunelli, C. A., Firpo, M. A., et al. (1995) · Biochemistry and Cell Biology · doi:10.1139/o95-093 · Cited by 52 · see citing works
The mRNA binding track in the Escherichia coli ribosome for mRNAs of different sequences
Bhangu, R., & Wollenzien, P. L. (1992) · Biochemistry · doi:10.1021/bi00140a033 · Cited by 52 · see citing works
Conformational Changes in the Ribosome Induced by Translational Miscoding Agents
Jerinic, O., & Joseph, S. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.4269 · Cited by 52 · see citing works
Garcı́a, C., Fortier, P.-L., Blanquet, S., et al. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.0395n.x · Cited by 48 · see citing works
Pactamycin resistance mutations in functional sites of 16 S rRNA
Mankin, A. S. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1387 · Cited by 47 · see citing works
Sette, M., Spurio, R., van Tilborg, P. J. A., et al. (1999) · RNA · doi:10.1017/s1355838299981487 · Cited by 47 · see citing works
Noah, J. W., Dolan, M. A., Babin, P., & Wollenzien, P. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.23.16576 · Cited by 46 · see citing works
Weiel, J., & Hershey, J. W. B. (1981) · Biochemistry · doi:10.1021/bi00523a032 · Cited by 46 · see citing works
Eisenstein, M., Shariv, I., Koren, G., et al. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0773 · Cited by 41 · see citing works
Photoincorporation of tetracycline into Escherichia coli ribosomes
Goldman, R. A., Cooperman, B. S., Strycharz, W. A., Williams, B. A., & Tritton, T. R. (1980) · FEBS Letters · doi:10.1016/0014-5793(80)81230-0 · Cited by 40 · see citing works
Binding Interaction between Tet(M) and the Ribosome: Requirements for Binding
Dantley, K. A., Dannelly, H. K., & Burdett, V. (1998) · Journal of Bacteriology · doi:10.1128/jb.180.16.4089-4092.1998 · Cited by 37 · see citing works
Firpo, M. A., Connelly, M. B., Goss, D. J., & Dahĺberg, A. E. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.9.4693 · Cited by 35 · see citing works
Photochemical cross-linking of initiation factor-3 to Escherichia coli 30 S ribosomal subunits.
MacKeen, L. A., Kahan, L., Wahba, A., & Schwartz, I. S. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)70495-5 · Cited by 34 · see citing works
Cock, E. D., Springer, M., & Dardel, F. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01350.x · Cited by 34 · see citing works
Shapkina, T. G., Dolan, M., Babin, P. R., et al. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3774 · Cited by 33 · see citing works
Bruhns, J., & Gualerzi, C. O. (1980) · Biochemistry · doi:10.1021/bi00549a023 · Cited by 33 · see citing works
Base changes at position 792 of Escherichia coli 16S rRNA affect assembly of 70S ribosomes.
Santer, M., Bennett‐Guerrero, E., Byahatti, S., et al. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.10.3700 · Cited by 31 · see citing works
Ringquist, S., Cunningham, P. R., Weitzmann, C. J., et al. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1560 · Cited by 18 · see citing works
Binding properties of a neurotoxin from the venom of the green mamba, Dendroaspis viridis.
Patrick, J., Stallcup, W. B., Zavanelli, M., et al. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)86206-3 · Cited by 17 · see citing works
Altamura, S., Sanz, J. L., Amils, R., et al. (1988) · Systematic and Applied Microbiology · doi:10.1016/s0723-2020(88)80004-3 · Cited by 17 · see citing works
Kurylo-Borowska, Z., & Sedkowska, J. (1974) · Biochimica et Biophysica Acta (BBA) - Protein Structure · doi:10.1016/0005-2795(74)90064-6 · Cited by 16 · see citing works
Biosynthesis of eideine:II. Localization of edeine synthetase within Bacillus brevis Vm4
Kurylo-Borowska, Z. (1975) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(75)90208-1 · Cited by 16 · see citing works
Herrera, F., Moreno, N., & MARTÍNEZ, J. A. (1984) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1984.tb08559.x · Cited by 8 · see citing works
TETRACYCLINE CHELATED MG2+-ION INITIATES HELIX UNWINDING FOR TET REPRESSOR INDUCTION
Orth, P., Saenger, W., & Hinrichs, W. (1998) · Worldwide Protein Data Bank · doi:10.2210/pdb1bj0/pdb · Cited by 2 · see citing works
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Wilson, D. N. (2014) · Nature Reviews Microbiology · doi:10.1038/nrmicro3155 · Cited by 1,054 · see citing works
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Connell, S. R., Tracz, D. M., Nierhaus, K. H., & Taylor, D. E. (2003) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.47.12.3675-3681.2003 · Cited by 449 · see citing works
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 · see citing works
The bacterial translation stress response.
Starosta, A. L., Lassak, J., Jung, K., & Wilson, D. N. (2014) · FEMS Microbiology Reviews · doi:10.1111/1574-6976.12083 · Cited by 210 · see citing works
Structural basis for TetM-mediated tetracycline resistance
Dönhöfer, A., Franckenberg, S., Wickles, S., Berninghausen, O., Beckmann, R., & Wilson, D. N. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1208037109 · Cited by 217 · see citing works
Retapamulin-Assisted Ribosome Profiling Reveals the Alternative Bacterial Proteome
Meydan, S., Marks, J., Klepacki, D., Sharma, V., Baranov, P. V., Firth, A. E., Margus, T., Kefi, A., Vázquez-Laslop, N., & Mankin, A. S. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.02.017 · Cited by 184 · see citing works
Functional, biophysical, and structural bases for antibacterial activity of tigecycline
Olson, M. W., Ruzin, A., Feyfant, E., Rush, T. S., O'Connell, J., & Bradford, P. A. (2006) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01499-05 · Cited by 207 · see citing works
Jenner, L., Starosta, A. L., Terry, D. S., Mikolajka, A., Filonava, L., Yusupov, M., Blanchard, S. C., Wilson, D. N., & Yusupova, G. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1216691110 · Cited by 204 · see citing works
Mutations in the 16S rRNA Genes of<i>Helicobacter pylori</i>Mediate Resistance to Tetracycline
Trieber, C. A., & Taylor, D. E. (2002) · Journal of Bacteriology · doi:10.1128/jb.184.8.2131-2140.2002 · Cited by 174 · see citing works
Target- and resistance-based mechanistic studies with TP-434, a novel fluorocycline antibiotic
Grossman, T. H., Starosta, A. L., Fyfe, C., O'Brien, W., Rothstein, D. M., Mikolajka, A., Wilson, D. N., & Sutcliffe, J. A. (2012) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.06187-11 · Cited by 162 · see citing works
16S rRNA Mutation-Mediated Tetracycline Resistance in <i>Helicobacter pylori</i>
Gerrits, M. M., de Zoete, M. R., Arents, N. L. A., Kuipers, E. J., & Kusters, J. G. (2002) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.46.9.2996-3000.2002 · Cited by 137 · see citing works
Mechanism of Tet(O)‐mediated tetracycline resistance
Connell, S. R., Trieber, C. A., Dinos, G. P., Einfeldt, E., Taylor, D. E., & Nierhaus, K. H. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg093 · Cited by 127 · see citing works
Structural conservation of antibiotic interaction with ribosomes
Paternoga, H., Crowe-McAuliffe, C., Bock, L. V., Koller, T. O., Morici, M., Beckert, B., Myasnikov, A. G., Grubmüller, H., Nováček, J., & Wilson, D. N. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01047-y · Cited by 94 · see citing works
Dailidiene, D., Bertoli, M. T., Miciuleviciene, J., Mukhopadhyay, A. K., Dailide, G., Pascasio, M. A., Kupcinskas, L., & Berg, D. E. (2002) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.46.12.3940-3946.2002 · Cited by 101 · see citing works
Yassin, A., Fredrick, K., & Mankin, A. S. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508444102 · Cited by 83 · see citing works
Negamycin interferes with decoding and translocation by simultaneous interaction with rRNA and tRNA
Polikanov, Y. S., Szal, T., Jiang, F., Gupta, P., Matsuda, R., Shiozuka, M., Steitz, T. A., Vázquez-Laslop, N., & Mankin, A. S. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.09.021 · Cited by 57 · see citing works
Cocozaki, A. I., Altman, R. B., Huang, J., Buurman, E. T., Kazmirski, S. L., Doig, P., Prince, D. B., Blanchard, S. C., Cate, J. H. D., & Ferguson, A. D. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1605127113 · Cited by 56 · see citing works
Nonaka, L., Connell, S. R., & Taylor, D. E. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.11.3708-3712.2005 · Cited by 55 · see citing works
Sarecycline interferes with tRNA accommodation and tethers mRNA to the 70S ribosome
Batool, Z., Lomakin, I. B., Polikanov, Y. S., & Bunick, C. G. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2008671117 · Cited by 50 · see citing works
A distinct translation initiation mechanism generates cryptic peptides for immune surveillance
Starck, S. R., Ow, Y., Jiang, V., Tokuyama, M., Rivera, M., Qi, X., Roberts, R. W., & Shastri, N. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003460 · Cited by 48 · see citing works
Olivier, N. B., Altman, R. B., Noeske, J., Basarab, G. S., Code, E., Ferguson, A. D., Gao, N., Huang, J., Juette, M. F., Livchak, S., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1414401111 · Cited by 48 · see citing works
Connell, S. R., Trieber, C. A., Stelzl, U., Einfeldt, E., Taylor, D. E., & Nierhaus, K. H. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.03115.x · Cited by 42 · see citing works
The impact of the stringent response on TRAFAC GTPases and prokaryotic ribosome assembly.
Bennison, D. J., Irving, S. E., & Corrigan, R. M. (2019) · Cells · doi:10.3390/cells8111313 · Cited by 37 · see citing works
Structural basis for differential inhibition of eukaryotic ribosomes by tigecycline
Li, X., Wang, M., Denk, T., Buschauer, R., Li, Y., Beckmann, R., & Cheng, J. (2024) · Nature Communications · doi:10.1038/s41467-024-49797-7 · Cited by 21 · see citing works
Chimeras of bacterial translation factors Tet(O) and EF‐G
Thakor, N. S., Nechifor, R., Scott, P. G., Keelan, M., Taylor, D. E., & Wilson, K. S. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.03.023 · Cited by 4 · see citing works
- Authors
- Pioletti, M., Schlünzen, F., Harms, J., Zarivach, R., Glühmann, M., Avila, H., Bashan, A., Bartels, H., Auerbach, T., Jacobi, C., Hartsch, T., Yonath, A., & Franceschi, F.
- Affiliations
- Max Planck Institute for Molecular Genetics (DE)
- Weizmann Institute of Science (IL)
- University of Göttingen (DE)
- Venue
- The EMBO Journal
- Published
- 2001-04-17
- Volume
- 20
- Issue
- 8
- Pages
- 1829-1839
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC125237
- OpenAlex
- W2124433456
- Cited by
- 527
- References
- 73
- Citations by year
- 2026: 8 · 2025: 10 · 2024: 18 · 2023: 14 · 2022: 17 · 2021: 24 · 2020: 7 · 2019: 15 · 2018: 17 · 2017: 13 · 2016: 28 · 2015: 14 · 2014: 23 · 2013: 19 · 2012: 19
- FWCI
- 11.55
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The EMBO Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- GRO (submittedVersion)
- Funders
- European Synchrotron Radiation Facility
- Max-Planck-Gesellschaft
- National Institutes of Health (GM34360)
- Deutsches Elektronen-Synchrotron
- National Institute of General Medical Sciences (GM-34360, R01GM034360)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA modifications and cancer
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- small ribosomal subunit, tetracycline, edeine, Thermus thermophilus, P-site tRNA, initiation complex, ribosome structure, protein synthesis initiation
- MeSH terms
- Binding Sites, Edeine, Models, Molecular, Peptide Chain Initiation, Translational, Peptide Initiation Factors, Protein Synthesis Inhibitors, Ribosomes, Tetracycline, Thermus thermophilus, Crystallography, X-Ray, Eukaryotic Initiation Factor-3
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