A novel single amino acid change in small subunit ribosomal protein S5 has profound effects on translational fidelity
Open accessAbstract
S5 is a small subunit ribosomal protein (r-protein) linked to the functional center of the 30S ribosomal subunit. In this study we have identified a unique amino acid mutation in Escherichia coli S5 that produces spectinomycin-resistance and cold sensitivity. This mutation significantly alters cell growth, folding of 16S ribosomal RNA, and translational fidelity. While translation initiation is not affected, both +1 and −1 frameshifting and nonsense suppression are greatly enhanced in the mutant strain. Interestingly, this S5 ribosome ambiguity-like mutation is spatially remote from previously identified S5 ribosome ambiguity (ram) mutations. This suggests that the mechanism responsible for ram phenotypes in the novel mutant strain is possibly distinct from those proposed for other known S5 (and S4) ram mutants. This study highlights the importance of S5 in ribosome function and cell physiology, and suggests that translational fidelity can be regulated in multiple ways.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Ring I of tetracycline forms van der Waals stacking interactions with the guanidinium group of residue R29 from ribosomal protein S5.
“Ring I of tetracycline also forms van der Waals stacking interactions with the guanidinium group of residue R29 from ribosomal protein S5 (21).”
From Resistance mutations generate divergent antibiotic susceptibility profiles against translation inhibitors (2016) · cites this paper as [21]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Molecular Cloning: A Laboratory Manual
Sambrook, J., Fritsch, E., & Maniatis, T. (1989) · UCLA - Biblioteca de Ciencias de la Salud · Cited by 133,589 · see citing works
Studies on transformation of Escherichia coli with plasmids
Hanahan, D. (1983) · Journal of Molecular Biology · doi:10.1016/s0022-2836(83)80284-8 · Cited by 11,274 · 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
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 · see citing works
Carter, 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
Structures of the Bacterial Ribosome at 3.5 A Resolution
Schuwirth, B. S., Borovinskaya, M. A., Hau, C. W., Zhang, W., Vila‐Sanjurjo, A., Holton, J. M., & Cate, J. H. D. (2005) · Science · doi:10.1126/science.1117230 · Cited by 1,417 · 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
Ribosome Structure and the Mechanism of Translation
Ramakrishnan, V. (2002) · Cell · doi:10.1016/s0092-8674(02)00619-0 · Cited by 932 · see citing works
Selection of tRNA by the Ribosome Requires a Transition from an Open to a Closed Form
Ogle, J. M., Murphy, F. V., Tarry, M. J., & Ramakrishnan, V. (2002) · Cell · doi:10.1016/s0092-8674(02)01086-3 · Cited by 663 · see citing works
The Path of Messenger RNA through the Ribosome
Yusupova, G. Z., Yusupov, M., Cate, J. H. D., & Noller, H. F. (2001) · Cell · doi:10.1016/s0092-8674(01)00435-4 · Cited by 597 · see citing works
Moazed, D., Stern, S., & Noller, H. F. (1986) · Journal of Molecular Biology · doi:10.1016/0022-2836(86)90441-9 · Cited by 544 · see citing works
Assembly Mapping of 30S Ribosomal Proteins from E. coli
Mizushima, S., & Nomura, M. (1970) · Nature · doi:10.1038/2261214a0 · Cited by 541 · see citing works
Carson, M. (1997) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(97)77027-7 · Cited by 510 · 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
Transfer RNA shields specific nucleotides in 16S ribosomal RNA from attack by chemical probes
Moazed, D., & Noller, H. F. (1986) · Cell · doi:10.1016/0092-8674(86)90813-5 · Cited by 420 · see citing works
Insights into the decoding mechanism from recent ribosome structures
Ogle, J. M., Carter, A. P., & Ramakrishnan, V. (2003) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(03)00066-5 · Cited by 372 · see citing works
Brodersen, D. E., Clemons, W., Carter, A. P., Wimberly, B. T., & Ramakrishnan, V. (2002) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5359 · Cited by 363 · see citing works
Woese, C. R., Magrum, L. J., Gupta, R., Siegel, R. B., Stahl, D. A., Kop, J., Crawford, N. M., Brosius, R., Gutell, R. R., Hogan, J. J., et al. (1980) · Nucleic Acids Research · doi:10.1093/nar/8.10.2275 · Cited by 346 · see citing works
Model for the three-dimensional folding of 16 S ribosomal RNA
Stern, S., Weiser, B., & Noller, H. F. (1988) · Journal of Molecular Biology · doi:10.1016/0022-2836(88)90588-8 · Cited by 304 · see citing works
Moazed, D., & Noller, H. F. (1990) · Journal of Molecular Biology · doi:10.1016/0022-2836(90)90016-f · Cited by 292 · see citing works
A functional pseudoknot in 16S ribosomal RNA.
Powers, T., & Noller, H. F. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07756.x · Cited by 286 · see citing works
Antibiotic resistance mutations in 16S and 23S ribosomal RNA genes ofEscherichia coli
Sigmund, C. D., Ettayebi, M., & Morgan, E. A. (1984) · Nucleic Acids Research · doi:10.1093/nar/12.11.4653 · Cited by 246 · see citing works
Structure-based analysis of protein-RNA interactions using the program ENTANGLE
Allers, J., & Shamoo, Y. E. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4857 · Cited by 242 · see citing works
Structure and Function of Ribosomes and Their Molecular ComponentsPreprint
Nomura, M., Mizushima, S.-I., Ozaki, M., Traub, P., & Lowry, C. V. (1969) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.1969.034.01.009 · Cited by 204 · see citing works
Guthrie, C., Nashimoto, H., & Nomura, M. (1969) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.63.2.384 · Cited by 186 · see citing works
Carson, M. (1997) · PubMed · Cited by 178 · see citing works
Dammel, C., & Noller, H. F. (1995) · Genes & Development · doi:10.1101/gad.9.5.626 · Cited by 161 · see citing works
The structure of ribosomal protein S5 reveals sites of interaction with 16S rRNA
Ramakrishnan, V., & White, S. W. (1992) · Nature · doi:10.1038/358768a0 · Cited by 152 · see citing works
Ribosomal Protein Conferring Sensitivity to the Antibiotic Spectinomycin in Escherichia coli
Bollen, A., DAVIES, J. E., OZAKI, M., & Mizushima, S.-I. (1969) · Science · doi:10.1126/science.165.3888.85 · Cited by 137 · see citing works
O'Connor, M. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.6.1185 · Cited by 129 · see citing works
Allen, P. N., & Noller, H. F. (1989) · Journal of Molecular Biology · doi:10.1016/0022-2836(89)90509-3 · Cited by 120 · see citing works
Culver, G. M., & Noller, H. F. (1999) · RNA · doi:10.1017/s1355838299990714 · Cited by 119 · see citing works
Self-citationStructure and function of bacterial ribosomes
Nashimoto, H., Held, W. A., Kaltschmidt, E., & Nomura, M. (1971) · Journal of Molecular Biology · doi:10.1016/0022-2836(71)90135-5 · Cited by 115 · see citing works
Merryman, C., Moazed, D., Daubresse, G., & Noller, H. F. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2243 · Cited by 110 · see citing works
Interaction of ribosomal proteins S5, S6, S11, S12, S18 and S21 with 16 S rRNA
Stern, S., Powers, T., Changchien, L., & Noller, H. F. (1988) · Journal of Molecular Biology · doi:10.1016/0022-2836(88)90467-6 · Cited by 106 · see citing works
Limitations of translational accuracy
Cg, K., Hughes, D., & Ehrenberg, M. (1996) · Cited by 100 · see citing works
A DNA fragment containing the groE genes can suppress mutations in the Escherichia coli dnaA gene
Jenkins, A., March, J. B., Oliver, I. R., & Masters, M. (1986) · Molecular and General Genetics MGG · doi:10.1007/bf00333275 · Cited by 94 · see citing works
The DnaK Chaperone System Facilitates 30S Ribosomal Subunit Assembly
Maki, J. A., Schnobrich, D. J., & Culver, G. M. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00562-2 · Cited by 92 · see citing works
Self-citationEffect of different mutaions in ribosomal protein S5 of Escherichia coli on translational fidelity
Piepersberg, W., Böck, A., & Wittmann, H. G. (1975) · Molecular and General Genetics MGG · doi:10.1007/bf00329777 · Cited by 86 · see citing works
Interaction of proteins S16, S17 and S20 with 16 S ribosomal RNA
Stern, S., Changchien, L., Craven, G. R., & Noller, H. F. (1988) · Journal of Molecular Biology · doi:10.1016/0022-2836(88)90241-0 · Cited by 78 · see citing works
Mapping structural differences between 30S ribosomal subunit assembly intermediates
Holmes, K., & Culver, G. M. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb719 · Cited by 69 · see citing works
Self-citationBrink, M. F., Brink, G., Verbeet, M., & de Boer, H. D. (1994) · Nucleic Acids Research · doi:10.1093/nar/22.3.325 · Cited by 69 · see citing works
Funatsu, G., Schiltz, E., & Wittmann, H. G. (1972) · Molecular and General Genetics MGG · doi:10.1007/bf00332781 · Cited by 67 · see citing works
Spectinomycin resistance at site 1192 in 16S ribosomal RNA of E. coli: an analysis of three mutants
Makosky, P. C., & Dahĺberg, A. E. (1987) · Biochimie · doi:10.1016/0300-9084(87)90216-1 · Cited by 62 · see citing works
Merryman, C., Moazed, D., McWhirter, J. R., & Noller, H. F. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2242 · Cited by 62 · see citing works
Itoh, T., & Wittmann, H. G. (1973) · Molecular and General Genetics MGG · doi:10.1007/bf00267779 · Cited by 57 · see citing works
[30] In vitro reconstitution of 30s ribosomal subunits using complete set of recombinant proteins
Culver, G. M., & Noller, H. F. (2000) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(00)18069-3 · Cited by 56 · see citing works
Self-citationFunatsu, G., Puls, W., Schiltz, E., Reinbolt, J., & Wittmann, H. G. (1972) · Molecular and General Genetics MGG · doi:10.1007/bf00277293 · Cited by 56 · see citing works
Piepersberg, W., Böck, A., Yaguchi, M., & Wittmann, H. G. (1975) · Molecular and General Genetics MGG · doi:10.1007/bf00269419 · Cited by 55 · see citing works
Probing the assembly of the 3′ major domain of 16 S rRNA
Powers, T., Stern, S., Changchien, L., & Noller, H. F. (1988) · Journal of Molecular Biology · doi:10.1016/0022-2836(88)90468-8 · Cited by 53 · see citing works
van Acken, U. (1975) · Molecular and General Genetics MGG · doi:10.1007/bf00268989 · Cited by 53 · see citing works
The primary structure of protein S5 from the small subunit of the Escherichia coli ribosome
Wittmann‐Liebold, B., & Greuer, B. (1978) · FEBS Letters · doi:10.1016/0014-5793(78)80059-3 · Cited by 52 · see citing works
Functional interactions between mutated forms of ribosomal proteins S4, S5 and S12
Andersson, D. I., Andersson, S. G. E., & Kurland, C. G. (1986) · Biochimie · doi:10.1016/s0300-9084(86)80164-x · Cited by 48 · see citing works
Assembly of the 30S ribosomal subunit: Positioning ribosomal protein S13 in the S7 assembly branch
Grondek, J. F., & Culver, G. M. (2004) · RNA · doi:10.1261/rna.7130504 · Cited by 36 · see citing works
Self-citationPoot, R. A., van den Worm, S. H. E., Pleij, C. W. A., & DUIN, J. V. (1998) · Nucleic Acids Research · doi:10.1093/nar/26.2.549 · Cited by 33 · see citing works
Changes in the primary structure of a mutationally altered ribosomal protein S 4 of Escherichia coli
Donner, D., & Kurland, C. G. (1972) · Molecular and General Genetics MGG · doi:10.1007/bf00272217 · Cited by 32 · see citing works
Nomura, M. (1987) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.1987.052.01.075 · Cited by 26 · see citing works
A role for proteins S3 and S14 in the 30 S ribosomal subunit.
Ramakrishnan, V., Graziano, V., & Capel, M. S. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)66827-9 · Cited by 19 · see citing works
A temperature sensitive mutant in Bacillus subtilis with an altered elongation factor G
Aharonowitz, Y., & Ron, E. Z. (1972) · Molecular and General Genetics MGG · doi:10.1007/bf00269132 · Cited by 19 · see citing works
DeWilde, M., & Wittmann‐Liebold, B. (1973) · Molecular and General Genetics MGG · doi:10.1007/bf00333767 · Cited by 13 · see citing works
Vladimirov, S. N., Graifer, D. M., Karpova, G. G., Semenkov, Y. P., Makhno, V. I., & KIRILLOV, S. V. (1985) · FEBS Letters · doi:10.1016/0014-5793(85)80294-5 · Cited by 13 · see citing works
Schnier, J. B., Isono, S., Cumberlidge, A. G., & Isono, K. (1985) · Molecular and General Genetics MGG · doi:10.1007/bf00330268 · Cited by 5 · see citing works
Flagged first, then by citations
1 of the 63 references couldn’t be matched to a known paper.
Research works printed but not linked: 1
- Merryman, C. and Noller, H.F. 1998. Footprinting and modification- interference analysis of binding sites on RNA. In RNA:Protein interactions, A practical approach (ed. C.W.J. Smith), pp. 237-253. Oxford University Press, New York.
Cited by
Sorted by citations
Ataluren as an Agent for Therapeutic Nonsense Suppression
Peltz, S. W., Morsy, M., Welch, E. M., & Jacobson, A. (2012) · Annual Review of Medicine · doi:10.1146/annurev-med-120611-144851 · Cited by 194 · see citing works
Ritchie, D. B., Foster, D. A. N., & Woodside, M. T. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1204114109 · Cited by 138 · see citing works
Hyperaccurate and Error-Prone Ribosomes Exploit Distinct Mechanisms during tRNA Selection
Zaher, H. S., & Green, R. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.06.009 · Cited by 107 · see citing works
Molecular mechanics of 30S subunit head rotation
Mohan, S., Donohue, J. P., & Noller, H. F. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1413731111 · Cited by 105 · see citing works
Costa, M., Borges, C. L., Bailão, A. M., Meirelles, G. V., Mendonça, Y. A., Dantas, S. F. I. M., de Faria, F. P., Felipe, M. S. S., Molinari-Madlum, E. E. W. I., Mendes‐Giannini, M. J. S., et al. (2007) · Microbiology · doi:10.1099/mic.0.2007/009332-0 · Cited by 85 · see citing works
The look-ahead effect of phenotypic mutations
Whitehead, D. J., Wilke, C. O., Vernazobres, D., & Bornberg-Bauer, E. (2008) · Biology Direct · doi:10.1186/1745-6150-3-18 · Cited by 84 · see citing works
Unemo, M., Golparian, D., Skogen, V., Olsen, A. O., Moi, H., Syversen, G., & Hjelmevoll, S. O. (2012) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01775-12 · Cited by 80 · see citing works
Chaudhuri, S., Vyas, K., Kapasi, P., Komar, A. A., Dinman, J. D., Barik, S., & Mazumder, B. (2007) · RNA · doi:10.1261/rna.694007 · Cited by 75 · see citing works
The ribosome structure controls and directs mRNA entry, translocation and exit dynamics
Kürkçüoğlu, Ö., Doruker, P., Sen, T. Z., Kloczkowski, A., & Jernigan, R. L. (2008) · Physical Biology · doi:10.1088/1478-3975/5/4/046005 · Cited by 67 · see citing works
Roy‐Chaudhuri, B., Kirthi, N., & Culver, G. M. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0912305107 · Cited by 60 · see citing works
Self-citationThe ribosome and the mechanism of protein synthesis
Frank, J., & Spahn, C. M. T. (2006) · Reports on Progress in Physics · doi:10.1088/0034-4885/69/5/r03 · Cited by 59 · 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
Roy‐Chaudhuri, B., Kirthi, N., Kelley, T., & Culver, G. M. (2008) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06252.x · Cited by 56 · see citing works
Self-citationProtein Assistants of Small Ribosomal Subunit Biogenesis in Bacteria
Maksimova, E. M., Kravchenko, O. V., Korepanov, A. P., & Stolboushkina, E. A. (2022) · Microorganisms · doi:10.3390/microorganisms10040747 · Cited by 27 · see citing works
Yang, Z., Guo, Q., Goto, S., Chen, Y., Li, N., Yan, K., Zhang, Y., Muto, A., Deng, H., Himeno, H., et al. (2014) · Protein & Cell · doi:10.1007/s13238-014-0044-1 · Cited by 28 · see citing works
Gupta, N., & Culver, G. M. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2887 · Cited by 26 · see citing works
Self-citationKthiri, F., Gautier, V., Le, H.-T., Prère, M. F., Fayet, O., Malki, A., Landoulsi, A., & Richarme, G. (2010) · Journal of Bacteriology · doi:10.1128/jb.01077-10 · Cited by 24 · see citing works
Halma, M. T. J., Ritchie, D. B., & Woodside, M. T. (2021) · Physical Review Letters · doi:10.1103/physrevlett.126.038102 · Cited by 24 · see citing works
Debroy, R., & Ramaiah, S. (2023) · World Journal of Microbiology and Biotechnology · doi:10.1007/s11274-023-03634-z · Cited by 20 · see citing works
Vallabhaneni, H., & Farabaugh, P. J. (2009) · RNA · doi:10.1261/rna.1530509 · Cited by 20 · see citing works
Yan, L. E., Su, J., Wang, Z., Yan, X., & Yu, R. (2017) · Journal of Ocean University of China · doi:10.1007/s11802-017-3339-z · Cited by 18 · see citing works
Targeted codon optimization improves translational fidelity for an Fc fusion protein
Hutterer, K. M., Zhang, Z., Michaels, M. L., Belouski, E., Hong, R. W., Shah, B., Berge, M., Barkhordarian, H., Le, E., Smith, S., et al. (2012) · Biotechnology and Bioengineering · doi:10.1002/bit.24555 · Cited by 17 · see citing works
Parente, J. A., Borges, C. L., Bailão, A. M., Felipe, M. S. S., Pereira, M., & Soares, C. M. D. A. (2008) · Mycopathologia · doi:10.1007/s11046-007-9078-8 · Cited by 15 · see citing works
Genome Engineering Using Targeted Oligonucleotide Libraries and Functional Selection
Diner, E. J., Garza‐Sánchez, F., & Hayes, C. S. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-197-0_5 · Cited by 14 · see citing works
Kamath, D. V., Gregory, S. T., & O'Connor, M. (2016) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01186-16 · Cited by 12 · see citing works
Ribosomal Protein Rps26 Influences 80S Ribosome Assembly in Saccharomyces cerevisiae
Belyy, A., Levanova, N., Tabakova, I., Rospert, S., & Belyi, Y. (2016) · mSphere · doi:10.1128/msphere.00109-15 · Cited by 10 · see citing works
Identification of Functional Interactome of Colistin Resistance Protein MCR-1 in Escherichia coli
Li, H., Wang, Y., Chen, Q., Xia, X., Shen, J., Wang, Y., & Shao, B. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.583185 · Cited by 9 · see citing works
Xia, W., Zhang, L., & Wang, J. (2022) · Foods · doi:10.3390/foods11203196 · Cited by 9 · see citing works
Ribosomal mutations affecting the translation of genes that use non‐optimal codons
Pelchovich, G., Sigal, N., Dana, A., Tuller, T., Bravo, I. G., & Gophna, U. (2014) · FEBS Journal · doi:10.1111/febs.12892 · Cited by 9 · see citing works
Chang, K., Salawu, E. O., Chang, Y.-Y., Wen, J., & Yang, L. (2018) · Bioinformatics · doi:10.1093/bioinformatics/bty762 · Cited by 9 · see citing works
Tang, N., Zhang, W., Chen, L., Wang, Y., & Tang, D. (2021) · Journal of the American Society for Horticultural Science · doi:10.21273/jashs05074-21 · Cited by 8 · see citing works
Korry, B. J., Lee, S. Y. E., Chakrabarti, A. K., Choi, A. H., Ganser, C., Machan, J. T., & Belenky, P. A. (2021) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00891-21 · Cited by 8 · see citing works
Suriyanarayanan, B., Lakshmi, P. P., Santhosh, R. S., Dhevendaran, K., Priya, B., & Krishna, S. (2015) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2015.1073633 · Cited by 8 · see citing works
Rational elicitation of cold-sensitive phenotypes
Baliga, C., Majhi, S., Mondal, K., Bhattacharjee, A., VijayRaghavan, K., & Varadarajan, R. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1604190113 · Cited by 8 · see citing works
Bheemireddy, S., Sandhya, S., & Srinivasan, N. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.654164 · Cited by 5 · see citing works
Chang, K. (2012) · Computational and Mathematical Methods in Medicine · doi:10.1155/2012/569870 · Cited by 5 · see citing works
Non-ribosomal Ribosome Assembly Factors in Escherichia coli
Choi, E., & Hwang, J. (2014) · Journal of Life Science · doi:10.5352/jls.2014.24.8.915 · Cited by 4 · see citing works
Antibiotic Resistance Mechanisms, with an Emphasis on Those Related to the Ribosome
Long, K. S., & Vester, B. (2008) · EcoSal Plus · doi:10.1128/ecosalplus.2.5.7 · Cited by 4 · see citing works
Warner, B. R., Bundschuh, R. A., & Fredrick, K. L. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad316 · Cited by 4 · see citing works
Ribosomal protein S5, ribosome biogenesis and translational fidelity
Roy‐Chaudhuri, B., Kirthi, N., Kelley, T., & Culver, G. M. (2011) · Springer eBooks · doi:10.1007/978-3-7091-0215-2_21 · Cited by 2 · see citing works
Self-citationPrangsuwan, P., Yinsai, O., Roytrakul, S., & Duangsonk, K. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms27010128 · Cited by 1 · see citing works
Structural Basis for the Decoding Mechanism
Gregory, S. T. (2009) · EcoSal Plus · doi:10.1128/ecosalplus.2.5.4 · Cited by 1 · see citing works
Mutations in ribosomal protein uS5 alter translation fidelity and mutagenesis in Pseudomonas putida
Jürgenstein, K., Ilves, H., Luhaäär, C., Brauer, A., Rèmme, J., & Kivisaar, M. (2025) · Journal of Bacteriology · doi:10.1128/jb.00334-25
Kanwal, M., Bilal, M., Faheem, M. Q., Awan, U. A., Mohamed, R. A. E. H., Alwethaynani, M. S., Binsaleh, A. Y., Fallatah, D. I., Alghamdi, A. M., Aziz, T., et al. (2026) · Open Medicine · doi:10.1515/med-2026-1547
- Authors
- Kirthi, N., Roy-Chaudhuri, B., Kelley, T., & Culver, G. M.
- Affiliations
- Iowa State University (US)
- Venue
- RNA
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2006-10-19
- Volume
- 12
- Issue
- 12
- Pages
- 2080-2091
- ISSN
- 1355-8382 (ISSN-L)
- 1469-9001
- PMC
- PMC1664723
- OpenAlex
- W2159706908
- Cited by
- 46
- References
- 63
- Citations by year
- 2026: 2 · 2025: 2 · 2023: 2 · 2022: 2 · 2021: 5 · 2018: 1 · 2017: 1 · 2016: 4 · 2015: 1 · 2014: 5 · 2012: 5
- FWCI
- 1.50
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- RNA (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute of General Medical Sciences (R01GM062432, GM62432)
- 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 › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA modifications and cancer
- Keywords
- ribosomal protein S5, amino acid mutations, translation fidelity, spectinomycin resistance, cold sensitivity, nonsense suppression, Escherichia coli
- MeSH terms
- Spectinomycin, Amino Acid Sequence, Escherichia coli, Glycine, Molecular Sequence Data, Mutation, Ribosomal Proteins, Ribosomes, RNA, Ribosomal, 16S, RNA, Transfer, Selection, Genetic, Protein Biosynthesis, Amino Acid Substitution, Drug Resistance, Bacterial, Escherichia coli Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review