{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T13:57:12Z","timestamp":1790776632258,"version":"4.1.0"},"reference-count":44,"publisher":"American Society for Microbiology","issue":"1","license":[{"start":{"date-parts":[[1998,1,1]],"date-time":"1998-01-01T00:00:00Z","timestamp":883612800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Antimicrob Agents Chemother"],"published-print":{"date-parts":[[1998,1]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            The effects of mutations in host genes on tetracycline resistance mediated by the Tet(O) and Tet(M) ribosomal protection proteins, which originated in\n            <jats:italic>Campylobacter<\/jats:italic>\n            spp. and\n            <jats:italic>Streptococcus<\/jats:italic>\n            spp., respectively, were investigated by using mutants of\n            <jats:italic>Salmonella typhimurium<\/jats:italic>\n            and\n            <jats:italic>Escherichia coli<\/jats:italic>\n            . The\n            <jats:italic>miaA<\/jats:italic>\n            ,\n            <jats:italic>miaB<\/jats:italic>\n            , and\n            <jats:italic>miaAB<\/jats:italic>\n            double mutants of\n            <jats:italic>S. typhimurium<\/jats:italic>\n            specify enzymes for tRNA modification at the adenosine at position 37, adjacent to the anticodon in tRNA. In\n            <jats:italic>S. typhimurium<\/jats:italic>\n            , this involves biosynthesis of\n            <jats:italic>N<\/jats:italic>\n            <jats:sup>6<\/jats:sup>\n            -(4-hydroxyisopentenyl)-2-methylthioadenosine (ms\n            <jats:sup>2<\/jats:sup>\n            io\n            <jats:sup>6<\/jats:sup>\n            A). The\n            <jats:italic>miaA<\/jats:italic>\n            mutation reduced the level of tetracycline resistance mediated by both Tet(O) and Tet(M), but the latter showed a greater effect, which was ascribed to the isopentenyl (i\n            <jats:sup>6<\/jats:sup>\n            ) group or to a combination of the methylthioadenosine (ms\n            <jats:sup>2<\/jats:sup>\n            ) and i\n            <jats:sup>6<\/jats:sup>\n            groups but not to the ms\n            <jats:sup>2<\/jats:sup>\n            group alone (specified by\n            <jats:italic>miaB<\/jats:italic>\n            ). In addition, mutations in\n            <jats:italic>E. coli rpsL<\/jats:italic>\n            genes, generating both streptomycin-resistant and streptomycin-dependent strains, were also shown to reduce the level of tetracycline resistance mediated by Tet(O) and Tet(M). The single-site amino acid substitutions present in the\n            <jats:italic>rpsL<\/jats:italic>\n            mutations were pleiotropic in their effects on tetracycline MICs. These mutants affect translational accuracy and kinetics and suggest that Tet(O) and Tet(M) binding to the ribosome may be reduced or slowed in the\n            <jats:italic>E. coli rpsL<\/jats:italic>\n            mutants in which the S12 protein is altered. Data from both the\n            <jats:italic>miaA<\/jats:italic>\n            and\n            <jats:italic>rpsL<\/jats:italic>\n            mutant studies indicate a possible link between stability of the aminoacyl-tRNA in the ribosomal acceptor site and tetracycline resistance mediated by the ribosomal protection proteins.\n          <\/jats:p>","DOI":"10.1128\/aac.42.1.59","type":"journal-article","created":{"date-parts":[[2018,10,9]],"date-time":"2018-10-09T00:30:08Z","timestamp":1539045008000},"page":"59-64","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":23,"title":["Host Mutations (\n            <i>miaA<\/i>\n            and\n            <i>rpsL<\/i>\n            ) Reduce Tetracycline Resistance Mediated by Tet(O) and Tet(M)"],"prefix":"10.1128","volume":"42","author":[{"given":"Diane E.","family":"Taylor","sequence":"first","affiliation":[{"name":"<!--label omitted: 1-->Departments of Medical Microbiology &amp; Immunology1 and"},{"name":"<!--label omitted: 2-->Biological Sciences,2 University of Alberta, Edmonton, Alberta T6G 2H7, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Catharine A.","family":"Trieber","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Departments of Medical Microbiology &amp; Immunology1 and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gudrun","family":"Trescher","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Departments of Medical Microbiology &amp; Immunology1 and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michelle","family":"Bekkering","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Departments of Medical Microbiology &amp; Immunology1 and"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"crossref","first-page":"3669","DOI":"10.1002\/j.1460-2075.1994.tb06676.x","article-title":"Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus","volume":"13","author":"\u00c6varsson A.","year":"1994","unstructured":"\u00c6varsson A. 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