{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,5]],"date-time":"2026-09-05T14:22:39Z","timestamp":1788618159153,"version":"build-2803163510"},"reference-count":60,"publisher":"Oxford University Press (OUP)","issue":"6","license":[{"start":{"date-parts":[[2024,1,16]],"date-time":"2024-01-16T00:00:00Z","timestamp":1705363200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/pages\/standard-publication-reuse-rights"}],"funder":[{"name":"Japan Science and Technology Agency-Precursory Research for Embryonic Science and Technology","award":["JPMJPR20EG"],"award-info":[{"award-number":["JPMJPR20EG"]}]},{"DOI":"10.13039\/100009619","name":"AMED","doi-asserted-by":"publisher","award":["21fk0108093j0003"],"award-info":[{"award-number":["21fk0108093j0003"]}],"id":[{"id":"10.13039\/100009619","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2024,5,31]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>The rapid emergence of multi-drug-resistant bacteria has raised a serious public health concern. Therefore, new antibiotic developments have been highly desired. Here, we propose a new method to visualize antibiotic actions on translating ribosomes in the cell-free system under macromolecular crowding conditions by cryo-electron microscopy, designated as the DARC method: the Direct visualization of Antibiotic binding on Ribosomes in the Cell-free translation system. This new method allows for acquiring a more comprehensive understanding of the mode of action of antibiotics on the translation inhibition without ribosome purification. Furthermore, with the direct link to biochemical analysis at the same condition as cryo-EM observation, we revealed the evolution of 2-DOS aminoglycosides from dibekacin (DBK) to arbekacin (ABK) by acquiring the synthetic tailored anchoring motif to lead to stronger binding affinity to ribosomes. Our cryo-EM structures of DBK and ABK bound ribosomes in the cell-free environment clearly depicted a synthetic tailored \u03b3-amino-\u03b1-hydroxybutyryl (HABA) motif formed additional interactions with the ribosome enhancing antibiotic bindings. This new approach would be valuable for understanding the function of antibiotics for more efficient drug development.<\/jats:p>","DOI":"10.1093\/jb\/mvae002","type":"journal-article","created":{"date-parts":[[2024,1,16]],"date-time":"2024-01-16T18:29:05Z","timestamp":1705429745000},"page":"587-598","source":"Crossref","is-referenced-by-count":12,"title":["Direct visualization of ribosomes in the cell-free system revealed the functional evolution of aminoglycoside"],"prefix":"10.1093","volume":"175","author":[{"given":"Junta","family":"Tomono","sequence":"first","affiliation":[{"name":"Tohoku University Graduate School of Life Sciences, , 2-1-1 Katahira, Aoba-ku, Sendai, Miyagi 980-8577, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kosuke","family":"Asano","sequence":"additional","affiliation":[{"name":"Tohoku University Graduate School of Life Sciences, , 2-1-1 Katahira, Aoba-ku, Sendai, Miyagi 980-8577, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Takuma","family":"Chiashi","sequence":"additional","affiliation":[{"name":"Tohoku University Graduate School of Life Sciences, , 2-1-1 Katahira, Aoba-ku, Sendai, Miyagi 980-8577, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Masato","family":"Suzuki","sequence":"additional","affiliation":[{"name":"National Institute of Infectious Diseases Antimicrobial Resistance Research Center, , 4-2-1 Aoba-cho, Higashimurayama, Tokyo 189-0002, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Masayuki","family":"Igarashi","sequence":"additional","affiliation":[{"name":"Institute of Microbial Chemistry (BIKAKEN) , 3-14-23 Kamiosaki, Shinagawa-ku, Tokyo 141-0021, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yoshiaki","family":"Takahashi","sequence":"additional","affiliation":[{"name":"Institute of Microbial Chemistry (BIKAKEN) , 3-14-23 Kamiosaki, Shinagawa-ku, Tokyo 141-0021, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yoshikazu","family":"Tanaka","sequence":"additional","affiliation":[{"name":"Tohoku University Graduate School of Life Sciences, , 2-1-1 Katahira, Aoba-ku, Sendai, Miyagi 980-8577, Japan"},{"name":"Tohoku University The advanced center for innovations in next-generation medicine (INGEM), , 2-1 Seiryo-machi, Aoba-ku, Sendai, Miyagi 980-8573, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0299-9140","authenticated-orcid":false,"given":"Takeshi","family":"Yokoyama","sequence":"additional","affiliation":[{"name":"Tohoku University Graduate School of Life Sciences, , 2-1-1 Katahira, Aoba-ku, Sendai, Miyagi 980-8577, Japan"},{"name":"Tohoku University The advanced center for innovations in next-generation medicine (INGEM), , 2-1 Seiryo-machi, Aoba-ku, Sendai, Miyagi 980-8573, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2024,1,16]]},"reference":[{"key":"2024060710263145900_ref1","article-title":"Antimicrobial resistance: Tackling a crisis for the health and wealth of nations","author":"O\u2019Neill","year":"2014","journal-title":"The Review on Antimicrobial Resistance."},{"key":"2024060710263145900_ref2","volume-title":"TACKLING DRUG-RESISTANT INFECTIONS GLOBALLY: FINAL REPORT AND RECOMMENDATIONS THE REVIEW ON ANTIMICROBIAL RESISTANCE CHAIRED BY JIM O\u2019NEILL. The Review on Antimicrobial Resistance","author":"O\u2019Neill","year":"2016"},{"key":"2024060710263145900_ref3","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.molcel.2015.10.019","article-title":"Blast from the past: reassessing forgotten translation inhibitors, antibiotic selectivity, and resistance mechanisms to aid drug development","volume":"61","author":"Arenzh","year":"2016","journal-title":"Mol. Cell"},{"key":"2024060710263145900_ref4","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1038\/nrmicro3155","article-title":"Ribosome-targeting antibiotics and mechanisms of bacterial resistance","volume":"12","author":"Wilson","year":"2014","journal-title":"Nat Rev Microbiol"},{"key":"2024060710263145900_ref5","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1146\/annurev-biochem-062917-011942","article-title":"Ribosome-targeting antibiotics: modes of action, mechanisms of resistance, and implications for drug design","volume":"87","author":"Lin","year":"2018","journal-title":"Annu. Rev. Biochem."},{"key":"2024060710263145900_ref6","doi-asserted-by":"crossref","first-page":"870","DOI":"10.1038\/nrmicro1265","article-title":"The bacterial ribosome as a target for antibiotics","volume":"3","author":"Poehlsgaard","year":"2005","journal-title":"Nat. Rev. Microbiol."},{"key":"2024060710263145900_ref7","doi-asserted-by":"crossref","first-page":"897","DOI":"10.1126\/science.1060612","article-title":"(2001) recognition of cognate transfer RNA by the 30S ribosomal subunit","volume":"292","author":"Ogle","year":"1979","journal-title":"Science"},{"key":"2024060710263145900_ref8","doi-asserted-by":"crossref","first-page":"1722","DOI":"10.1126\/science.285.5434.1722","article-title":"(1999) recognition of the codon-anticodon helix by ribosomal RNA","volume":"285","author":"Yoshizawa","year":"1979","journal-title":"Science"},{"key":"2024060710263145900_ref9","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1038\/nsmb1271","article-title":"Structural basis for aminoglycoside inhibition of bacterial ribosome recycling","volume":"14","author":"Borovinskaya","year":"2007","journal-title":"Nat. Struct. Mol. Biol."},{"key":"2024060710263145900_ref10","doi-asserted-by":"crossref","first-page":"957","DOI":"10.1038\/nsmb.2360","article-title":"Allosteric control of the ribosome by small-molecule antibiotics","volume":"19","author":"Wang","year":"2012","journal-title":"Nat. Struct. Mol. Biol."},{"key":"2024060710263145900_ref11","doi-asserted-by":"crossref","first-page":"1234","DOI":"10.1038\/nature08403","article-title":"What recent ribosome structures have revealed about the mechanism of translation","volume":"461","author":"Schmeing","year":"2009","journal-title":"Nature"},{"key":"2024060710263145900_ref12","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1016\/S0968-0004(03)00066-5","article-title":"Insights into the decoding mechanism from recent ribosome structures","volume":"28","author":"Ogle","year":"2003","journal-title":"Trends Biochem. Sci."},{"key":"2024060710263145900_ref13","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1016\/j.celrep.2013.01.027","article-title":"The impact of aminoglycosides on the dynamics of translation elongation","volume":"3","author":"Tsai","year":"2013","journal-title":"Cell Rep."},{"key":"2024060710263145900_ref14","doi-asserted-by":"crossref","first-page":"66","DOI":"10.3181\/00379727-55-14461","article-title":"Streptomycin, a substance exhibiting antibiotic activity against gram-positive and gram-negative bacteria","volume":"55","author":"Schatz","year":"1944","journal-title":"Exp. Biol. Med."},{"key":"2024060710263145900_ref15","doi-asserted-by":"crossref","first-page":"4","DOI":"10.1038\/ja.2017.117","article-title":"Destination of aminoglycoside antibiotics in the \u2018post-antibiotic era\u2019","volume":"71","author":"Takahashi","year":"2018","journal-title":"J Antibiot (Tokyo)"},{"key":"2024060710263145900_ref16","doi-asserted-by":"crossref","first-page":"1089","DOI":"10.1126\/science.1176667","article-title":"Antibiotics for emerging pathogens","volume":"325","author":"Fischbach","year":"2009","journal-title":"Science"},{"key":"2024060710263145900_ref17","doi-asserted-by":"crossref","first-page":"340","DOI":"10.1038\/35030019","article-title":"Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics","volume":"407","author":"Carter","year":"2000","journal-title":"Nature"},{"key":"2024060710263145900_ref18","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1038\/s41592-020-01054-7","article-title":"Multi-particle cryo-EM refinement with M visualizes ribosome-antibiotic complex at 3.5 \u00c5 in cells","volume":"18","author":"Tegunov","year":"2021","journal-title":"Nat. Methods"},{"key":"2024060710263145900_ref19","doi-asserted-by":"crossref","first-page":"751","DOI":"10.1038\/90802","article-title":"Cell-free translation reconstituted with purified components","volume":"19","author":"Shimizu","year":"2001","journal-title":"Nat. Biotechnol."},{"key":"2024060710263145900_ref20","doi-asserted-by":"crossref","first-page":"760","DOI":"10.1016\/j.molcel.2009.05.014","article-title":"The ordered transcription of RNA domains is not essential for ribosome biogenesis in Escherichia coli","volume":"34","author":"Kitahara","year":"2009","journal-title":"Mol. Cell"},{"key":"2024060710263145900_ref21","doi-asserted-by":"crossref","first-page":"15386","DOI":"10.1073\/pnas.0605970103","article-title":"Comprehensive genetic selection revealed essential bases in the peptidyl-transferase center","volume":"103","author":"Sato","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"2024060710263145900_ref22","doi-asserted-by":"crossref","first-page":"3539","DOI":"10.1093\/nar\/gkn224","article-title":"Ribosomal RNAs are tolerant toward genetic insertions: evolutionary origin of the expansion segments","volume":"36","author":"Yokoyama","year":"2008","journal-title":"Nucleic Acids Res."},{"key":"2024060710263145900_ref23","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1016\/j.jsb.2005.07.007","article-title":"Automated electron microscope tomography using robust prediction of specimen movements","volume":"152","author":"Mastronarde","year":"2005","journal-title":"J. Struct. Biol."},{"key":"2024060710263145900_ref24","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.42166","article-title":"New tools for automated high-resolution cryo-EM structure determination in RELION-3","volume":"7","author":"Zivanov","year":"2018","journal-title":"elife"},{"key":"2024060710263145900_ref25","doi-asserted-by":"crossref","first-page":"216","DOI":"10.1016\/j.jsb.2015.08.008","article-title":"CTFFIND4: fast and accurate defocus estimation from electron micrographs","volume":"192","author":"Rohou","year":"2015","journal-title":"J. Struct. Biol."},{"key":"2024060710263145900_ref26","doi-asserted-by":"crossref","first-page":"1153","DOI":"10.1038\/s41592-019-0575-8","article-title":"Positive-unlabeled convolutional neural networks for particle picking in cryo-electron micrographs","volume":"16","author":"Bepler","year":"2019","journal-title":"Nat. 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J."},{"key":"2024060710263145900_ref31","doi-asserted-by":"crossref","first-page":"2126","DOI":"10.1107\/S0907444904019158","article-title":"Coot: model-building tools for molecular graphics","volume":"60","author":"Emsley","year":"2004","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"2024060710263145900_ref32","doi-asserted-by":"crossref","first-page":"1","DOI":"10.7554\/eLife.60482","article-title":"Structure of the bacterial ribosome at 2 \u00c5 resolution","volume":"9","author":"Watson","year":"2020","journal-title":"elife"},{"key":"2024060710263145900_ref33","first-page":"472","article-title":"Visualization of chemical modifications in the human 80S ribosome structure","volume":"551","author":"Natchiar","year":"2017","journal-title":"Nat. Cell Biol."},{"key":"2024060710263145900_ref34","doi-asserted-by":"crossref","first-page":"1074","DOI":"10.1107\/S0907444909029436","article-title":"Electronic ligand builder and optimization workbench (eLBOW): a tool for ligand coordinate and restraint generation","volume":"65","author":"Moriarty","year":"2009","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"2024060710263145900_ref35","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1107\/S0907444909052925","article-title":"PHENIX: a comprehensive python-based system for macromolecular structure solution","volume":"66","author":"Adams","year":"2010","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"2024060710263145900_ref36","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1002\/jcc.20084","article-title":"UCSF chimera--a visualization system for exploratory research and analysis","volume":"25","author":"Pettersen","year":"2004","journal-title":"J. Comput. Chem."},{"key":"2024060710263145900_ref37","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1002\/pro.3235","article-title":"UCSF chimera X: meeting modern challenges in visualization and analysis","volume":"27","author":"Goddard","year":"2018","journal-title":"Protein Sci."},{"key":"2024060710263145900_ref38","doi-asserted-by":"crossref","first-page":"485","DOI":"10.7164\/antibiotics.24.485","article-title":"3\u2032, 4\u2019-DIDEOXY-kanamycin b active against kanamycin-resistant ESCHERICHIA COLI and pseudomonas aeruginosa","volume":"24","author":"Umezawa","year":"1971","journal-title":"J Antibiot (Tokyo)"},{"key":"2024060710263145900_ref39","doi-asserted-by":"crossref","first-page":"412","DOI":"10.7164\/antibiotics.26.412","article-title":"SYNTHESES OF l-N-{(S)-4-AMINO-2-HYDROXYBUTYRYL}-KANAMYCIN B AND-3\u2032, 4\u2019-DIDEOXYKANAMYCIN B ACTIVE AGAINST KANAMYCIN-RESISTANT BACTERIA","volume":"26","author":"Kondo","year":"1973","journal-title":"J Antibiot (Tokyo)"},{"key":"2024060710263145900_ref40","doi-asserted-by":"crossref","first-page":"695","DOI":"10.7164\/antibiotics.25.695","article-title":"Bb-K 8, a new semisynthetic aminoglycoside antibiotic","volume":"25","author":"Kawaguchi","year":"1972","journal-title":"J Antibiot (Tokyo)"},{"key":"2024060710263145900_ref41","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1016\/j.drup.2010.08.003","article-title":"Aminoglycoside modifying enzymes","volume":"13","author":"Ramirez","year":"2010","journal-title":"Drug Resist. Updat."},{"key":"2024060710263145900_ref42","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1093\/jac\/dkq408","article-title":"Activity of aminoglycosides, including ACHN-490, against carbapenemresistant Enterobacteriaceae isolates","volume":"66","author":"Livermore","year":"2011","journal-title":"J. Antimicrob. Chemother."},{"key":"2024060710263145900_ref43","doi-asserted-by":"crossref","first-page":"797","DOI":"10.1128\/AAC.24.5.797","article-title":"Mechanism of action of Habekacin, a novel amino acid-containing aminoglycoside antibiotic","volume":"24","author":"Tanaka","year":"1983","journal-title":"Antimicrob. Agents Chemother."},{"key":"2024060710263145900_ref44","doi-asserted-by":"crossref","first-page":"6880","DOI":"10.1093\/nar\/gkab495","article-title":"Mechanistic insights into translation inhibition by aminoglycoside antibiotic arbekacin","volume":"49","author":"Parajuli","year":"2021","journal-title":"Nucleic Acids Res."},{"key":"2024060710263145900_ref45","doi-asserted-by":"crossref","first-page":"6437","DOI":"10.1093\/emboj\/17.22.6437","article-title":"Structural origins of gentamicin antibiotic action","volume":"17","author":"Yoshizawa","year":"1998","journal-title":"EMBO J."},{"key":"2024060710263145900_ref46","doi-asserted-by":"crossref","first-page":"340","DOI":"10.1038\/35030019","article-title":"Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics","volume":"407","author":"Carter","year":"2000","journal-title":"Nature"},{"key":"2024060710263145900_ref47","doi-asserted-by":"crossref","first-page":"290","DOI":"10.1261\/rna.078188.120","article-title":"The landscape of translational stall sites in bacteria revealed by monosome and disome profiling","volume":"28","author":"Fujita","year":"2022","journal-title":"RNA"},{"key":"2024060710263145900_ref48","doi-asserted-by":"crossref","first-page":"1095","DOI":"10.1038\/s41467-023-36742-3","article-title":"The translating bacterial ribosome at 1.55 \u00c5 resolution generated by cryo-EM imaging services","volume":"14","author":"Fromm","year":"2023","journal-title":"Nat. Commun."},{"key":"2024060710263145900_ref49","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1038\/s41594-022-00723-9","article-title":"Structural basis for context-specific inhibition of translation by oxazolidinone antibiotics","volume":"29","author":"Tsai","year":"2022","journal-title":"Nat. Struct. Mol. Biol."},{"key":"2024060710263145900_ref50","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1016\/j.jmb.2004.11.073","article-title":"Mutagenesis of 16 S rRNA C1409-G1491 base-pair differentiates between 6\u2032OH and 6\u2032NH3+ aminoglycosides","volume":"346","author":"Pfister","year":"2005","journal-title":"J. Mol. Biol."},{"key":"2024060710263145900_ref51","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1038\/nature13737","article-title":"Structural basis for the inhibition of the eukaryotic ribosome","volume":"513","author":"De Loubresse","year":"2014","journal-title":"Nature"},{"key":"2024060710263145900_ref52","doi-asserted-by":"crossref","first-page":"358","DOI":"10.1016\/j.jmb.2006.03.038","article-title":"Aminoglycoside resistance by arm A-mediated ribosomal 16 S methylation in human bacterial pathogens","volume":"359","author":"Liou","year":"2006","journal-title":"J. Mol. Biol."},{"key":"2024060710263145900_ref53","doi-asserted-by":"crossref","first-page":"48","DOI":"10.3389\/fmolb.2018.00048","article-title":"The mechanisms of action of ribosome-targeting peptide antibiotics","volume":"5","author":"Polikanov","year":"2018","journal-title":"Front. Mol. Biosci."},{"key":"2024060710263145900_ref54","doi-asserted-by":"crossref","first-page":"5112","DOI":"10.1128\/AAC.49.12.5112-5118.2005","article-title":"Analysis of the contribution of individual substituents in 4,6-aminoglycoside-ribosome interaction","volume":"49","author":"Hobbie","year":"2005","journal-title":"Antimicrob. Agents Chemother."},{"key":"2024060710263145900_ref55","doi-asserted-by":"crossref","first-page":"741","DOI":"10.1038\/s41586-021-03713-x","article-title":"Structural basis of early translocation events on the ribosome","volume":"595","author":"Rundlet","year":"2021","journal-title":"Nature"},{"key":"2024060710263145900_ref56","doi-asserted-by":"crossref","first-page":"618","DOI":"10.1074\/jbc.M109959200","article-title":"Megalin deficiency offers protection from renal aminoglycoside accumulation *","volume":"277","author":"Schmitz","year":"2002","journal-title":"J. Biol. Chem."},{"key":"2024060710263145900_ref57","doi-asserted-by":"crossref","first-page":"10984","DOI":"10.1073\/pnas.1204073109","article-title":"Dissociation of antibacterial activity and aminoglycoside ototoxicity in the 4-monosubstituted 2-deoxystreptamine apramycin","volume":"109","author":"Matt","year":"2012","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"2024060710263145900_ref58","doi-asserted-by":"crossref","first-page":"1957","DOI":"10.1038\/s41467-021-22251-8","article-title":"Beam image-shift accelerated data acquisition for near-atomic resolution single-particle cryo-electron tomography","volume":"12","author":"Bouvette","year":"2021","journal-title":"Nat. Commun."},{"key":"2024060710263145900_ref59","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1038\/s41592-022-01690-1","article-title":"Parallel cryo electron tomography on in situ lamellae","volume":"20","author":"Eisenstein","year":"2023","journal-title":"Nat. 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