{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T15:17:37Z","timestamp":1790522257482,"version":"4.1.0"},"reference-count":31,"publisher":"American Society for Microbiology","issue":"3","license":[{"start":{"date-parts":[[1999,2,1]],"date-time":"1999-02-01T00:00:00Z","timestamp":917827200000},"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":["J Bacteriol"],"published-print":{"date-parts":[[1999,2]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            The physiological function of a new gene, hereby designated\n            <jats:italic>merG<\/jats:italic>\n            , located between\n            <jats:italic>merA<\/jats:italic>\n            and\n            <jats:italic>merB<\/jats:italic>\n            on the broad-spectrum\n            <jats:italic>mer<\/jats:italic>\n            operon of\n            <jats:italic>Pseudomonas<\/jats:italic>\n            strain K-62 plasmid pMR26 was investigated. The 654-bp\n            <jats:italic>merG<\/jats:italic>\n            gene encodes a protein with a canonical leader sequence at its N terminus. The processing of the signal peptide of this protein was dose-dependently inhibited by sodium azide, a potent inhibitor of protein export. These results suggest that the mature MerG protein (ca. 20 kDa) may be located in the periplasm. Deletion of the\n            <jats:italic>merG<\/jats:italic>\n            gene from the broad-spectrum\n            <jats:italic>mer<\/jats:italic>\n            operon of pMR26 had no effect on the inorganic mercury resistance phenotype, but rendered the bacterium more sensitive to phenylmercury than its isogenic wild-type strain.\n            <jats:italic>Escherichia coli<\/jats:italic>\n            cells bearing pMU29, which carries a deletion of the\n            <jats:italic>merG<\/jats:italic>\n            gene, took up significantly more phenylmercury than the bacteria with the intact plasmid pMRA17. When the\n            <jats:italic>merG<\/jats:italic>\n            gene in a compatible plasmid was transformed into the\n            <jats:italic>E. coli<\/jats:italic>\n            strain carrying pMU29, the high uptake of and high sensitivity to phenylmercury were almost completely restored to their original levels. These results demonstrate that the\n            <jats:italic>merG<\/jats:italic>\n            gene is involved in phenylmercury resistance, presumably by reducing in-cell permeability to phenylmercury.\n          <\/jats:p>","DOI":"10.1128\/jb.181.3.726-730.1999","type":"journal-article","created":{"date-parts":[[2019,12,31]],"date-time":"2019-12-31T16:44:30Z","timestamp":1577810670000},"page":"726-730","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":47,"title":["The\n            <i>merG<\/i>\n            Gene Product Is Involved in Phenylmercury Resistance in\n            <i>Pseudomonas<\/i>\n            Strain K-62"],"prefix":"10.1128","volume":"181","author":[{"given":"Masako","family":"Kiyono","sequence":"first","affiliation":[{"name":"<!--label omitted: 1-->Faculty of Pharmaceutical Sciences, Setsunan University, Hirakata, Osaka 573-0101, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hidemitsu","family":"Pan-Hou","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Faculty of Pharmaceutical Sciences, Setsunan University, Hirakata, Osaka 573-0101, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"crossref","first-page":"400","DOI":"10.1016\/0968-0004(85)90069-6","article-title":"Bacterial resistance to mercury\u2014reductio ad absurdum?","volume":"10","author":"Brown N. 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