{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,22]],"date-time":"2026-10-22T22:07:54Z","timestamp":1792706874803,"version":"4.5.0"},"reference-count":29,"publisher":"Pharmaceutical Society of Japan","issue":"11","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biological &amp; Pharmaceutical Bulletin","Biol. Pharm. Bull."],"published-print":{"date-parts":[[2013]]},"DOI":"10.1248\/bpb.b13-00554","type":"journal-article","created":{"date-parts":[[2013,8,27]],"date-time":"2013-08-27T23:39:23Z","timestamp":1377646763000},"page":"1835-1841","source":"Crossref","is-referenced-by-count":62,"title":["Role of MerC, MerE, MerF, MerT, and\/or MerP in Resistance to Mercurials and the Transport of Mercurials in &lt;i&gt;Escherichia coli&lt;\/i&gt;"],"prefix":"10.1248","volume":"36","author":[{"given":"Yuka","family":"Sone","sequence":"first","affiliation":[{"name":"Department of Public Health and Molecular Toxicology, School of Pharmacy, Kitasato University"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ryosuke","family":"Nakamura","sequence":"additional","affiliation":[{"name":"Department of Public Health and Molecular Toxicology, School of Pharmacy, Kitasato University"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hidemitsu","family":"Pan-Hou","sequence":"additional","affiliation":[{"name":"Faculty of Pharmaceutical Sciences, Setsunan University"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tomoo","family":"Itoh","sequence":"additional","affiliation":[{"name":"Department of Public Health and Molecular Toxicology, School of Pharmacy, Kitasato University"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Masako","family":"Kiyono","sequence":"additional","affiliation":[{"name":"Department of Public Health and Molecular Toxicology, School of Pharmacy, Kitasato University"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"163","reference":[{"key":"1","doi-asserted-by":"crossref","unstructured":"1) Nies DH. Efflux-mediated heavy metal resistance in prokaryotes. <i>FEMS Microbiol. Rev.<\/i>, 27, 313\u2013339 (2003).","DOI":"10.1016\/S0168-6445(03)00048-2"},{"key":"2","doi-asserted-by":"crossref","unstructured":"2) Malik A. Metal bioremediation through growing cells. <i>Environ. Int.<\/i>, 30, 261\u2013278 (2004).","DOI":"10.1016\/j.envint.2003.08.001"},{"key":"3","unstructured":"3) McGrath SP, Zhao FJ. Phytoextraction of metals and metalloids from contaminated soils. <i>Curr. Opin. Biotechnol.<\/i>, 14, 277\u2013282 (2003)."},{"key":"4","unstructured":"4) Barkay T, Miller SM, Summers AO. Bacterial mercury resistance from atoms to ecosystems. <i>FEMS Microbiol. Rev.<\/i>, 27, 355\u2013384 (2003)."},{"key":"5","unstructured":"5) Silver S, Phung LT. Bacterial heavy metal resistance: new surprises. <i>Annu. Rev. Microbiol.<\/i>, 50, 753\u2013789 (1996)."},{"key":"6","unstructured":"6) Brown NL, Shih YC, Leang C, Glendinning KJ, Hobman JL, Wilson JR. Mercury transport and resistance. <i>Biochem. Soc. Trans.<\/i>, 30, 715\u2013718 (2002)."},{"key":"7","unstructured":"7) Liebert CA, Hall RM, Summers AO. Transposon Tn<i>21<\/i>, flagship of the floating genome. <i>Microbiol. Mol. Biol. Rev.<\/i>, 63, 507\u2013522 (1999)."},{"key":"8","doi-asserted-by":"crossref","unstructured":"8) Kiyono M, Omura T, Inuzuka M, Fujimori H, Pan-Hou H. Nucleotide sequence and expression of the organomercurial-resistance determinants from a <i>Pseudomonas<\/i> K-62 plasmid pMR26. <i>Gene<\/i>, 189, 151\u2013157 (1997).","DOI":"10.1016\/S0378-1119(96)00741-X"},{"key":"9","unstructured":"9) Kiyono M, Pan-Hou H. DNA sequence and expression of a defective <i>mer<\/i> operon from <i>Pseudomonas<\/i> K-62 plasmid pMR26. <i>Biol. Pharm. Bull.<\/i>, 22, 910\u2013914 (1999)."},{"key":"10","unstructured":"10) Kiyono M, Pan-Hou H. The <i>merG<\/i> gene product is involved in phenylmercury resistance in <i>Pseudomonas<\/i> strain K-62. <i>J. Bacteriol.<\/i>, 181, 726\u2013730 (1999)."},{"key":"11","unstructured":"11) Wilson JR, Leang C, Morby AP, Hobman JL, Brown NL. MerF is a mercury transport protein: different structures but a common mechanism for mercuric ion transporters? <i>FEBS Lett.<\/i>, 472, 78\u201382 (2000)."},{"key":"12","unstructured":"12) Mok T, Chen JS, Shlykov MA, Saier MH. Bioinformatic analyses of bacterial mercury ion (Hg<sup>2+<\/sup>) transporters. <i>Water Air Soil Pollut.<\/i>, 223, 4443\u20134457 (2012)."},{"key":"13","unstructured":"13) Sahlman L, Hagglof EM, Powlowski J. Roles of the four cysteine residues in the function of the integral inner membrane Hg<sup>2+<\/sup>-binding protein, MerC. <i>Biochem. Biophys. Res. Commun.<\/i>, 255, 307\u2013311 (1999)."},{"key":"14","unstructured":"14) Sahlman L, Wong W, Powlowski J. A mercuric ion uptake role for the integral inner membrane protein, MerC, involved in bacterial mercuric ion resistance. <i>J. Biol. Chem.<\/i>, 272, 29518\u201329526 (1997)."},{"key":"15","unstructured":"15) Rossy E, Seneque O, Lascoux D, Lemaire D, Crouzy S, Delangle P, Coves J. Is the cytoplasmic loop of MerT, the mercuric ion transport protein, involved in mercury transfer to the mercuric reductase? <i>FEBS Lett.<\/i>, 575, 86\u201390 (2004)."},{"key":"16","unstructured":"16) Schu\u00e9 M, Dover LG, Besra GS, Parkhill J, Brown NL. Sequence and analysis of a plasmid-encoded mercury resistance operon from <i>Mycobacterium marinum<\/i> identifies MerH, a new mercuric ion transporter. <i>J. Bacteriol.<\/i>, 191, 439\u2013444 (2009)."},{"key":"17","unstructured":"17) Krogh A, Larsson B, von Heijne G, Sonnhammer EL. Predicting transmembrane protein topology with a hidden Markov model. application to complete genomes. <i>J. Mol. Biol.<\/i>, 305, 567\u2013580 (2001)."},{"key":"18","doi-asserted-by":"crossref","unstructured":"18) Hashimoto-Gotoh T, Mizuno T, Ogasahara Y, Nakagawa M. An oligodeoxyribonucleotide-directed dual amber method for site-directed mutagenesis. <i>Gene<\/i>, 152, 271\u2013275 (1995).","DOI":"10.1016\/0378-1119(94)00750-M"},{"key":"19","unstructured":"19) Kiyono M, Sone Y, Nakamura R, Pan-Hou H, Sakabe K. The MerE protein encoded by transposon Tn<i>21<\/i> is a broad mercury transporter in <i>Escherichia coli<\/i>. <i>FEBS Lett.<\/i>, 583, 1127\u20131131 (2009)."},{"key":"20","unstructured":"20) Sone Y, Pan-Hou H, Nakamura R, Sakabe K, Kiyono M. Roles played by MerE and MerT in the transport of inorganic and organic mercury compounds in Gram-negative bacteria. <i>J. Health Sci.<\/i>, 56, 123\u2013127 (2010)."},{"key":"21","unstructured":"21) Takamatsu H, Hiraoka T, Kodama T, Koide H, Kozuka S, Tochikubo K, Watabe K. Cloning of a novel gene <i>yrbB<\/i>, encoding a protein located in the spore integument of <i>Bacillus subtilis<\/i>. <i>FEMS Microbiol. Lett.<\/i>, 166, 361\u2013367 (1998)."},{"key":"22","unstructured":"22) Suzuki T, Kanaya T, Okazaki H, Ogawa K, Usami A, Watanabe H, Kadono-Okuda K, Yamakawa M, Sato H, Mori H, Takahashi S, Oda K. Efficient protein production using a <i>Bombyx mori<\/i> nuclear polyhedrosis virus lacking the cysteine proteinase gene. <i>J. Gen. Virol.<\/i>, 78, 3073\u20133080 (1997)."},{"key":"23","doi-asserted-by":"crossref","unstructured":"23) Maeda S. Expression of foreign genes in insects using <i>Baculovirus<\/i> vectors. <i>Annu. Rev. Entomol.<\/i>, 34, 351\u2013372 (1989).","DOI":"10.1146\/annurev.en.34.010189.002031"},{"key":"24","unstructured":"24) Kiyono M, Sone Y, Miyahara K, Oka Y, Nakamura M, Nakamura R, Sato MH, Pan-Hou H, Sakabe K, Inoue K-i. Genetic expression of bacterial <i>merC<\/i> fused with plant SNARE in <i>Saccharomyces cerevisiae<\/i> increased mercury accumulation. <i>Biochem. Eng. J.<\/i>, 56, 137\u2013141 (2011)."},{"key":"25","unstructured":"25) Nagata T, Nakamura A, Akizawa T, Pan-Hou H. Genetic engineering of transgenic <i>tobacco<\/i> for enhanced uptake and bioaccumulation of mercury. <i>Biol. Pharm. Bull.<\/i>, 32, 1491\u20131495 (2009)."},{"key":"26","unstructured":"26) Morby AP, Hobman JL, Brown NL. The role of cysteine residues in the transport of mercuric ions by the Tn<i>501<\/i> MerT and MerP mercury-resistance proteins. <i>Mol. Microbiol.<\/i>, 17, 25\u201335 (1995)."},{"key":"27","unstructured":"27) Kiyono M, Omura H, Omura T, Murata S, Pan-Hou H. Removal of inorganic and organic mercurials by immobilized bacteria having <i>mer-ppk<\/i> fusion plasmids. <i>Appl. Microbiol. Biotechnol.<\/i>, 62, 274\u2013278 (2003)."},{"key":"28","unstructured":"28) Pan-Hou H, Kiyono M, Omura H, Omura T, Endo G. Polyphosphate produced in recombinant <i>Escherichia coli<\/i> confers mercury resistance. <i>FEMS Microbiol. Lett.<\/i>, 207, 159\u2013164 (2002)."},{"key":"29","unstructured":"29) Nagata T, Kiyono M, Pan-Hou H. Engineering expression of bacterial polyphosphate kinase in <i>tobacco<\/i> for mercury remediation. <i>Appl. Microbiol. Biotechnol.<\/i>, 72, 777\u2013782 (2006)."}],"container-title":["Biological and Pharmaceutical Bulletin"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.jstage.jst.go.jp\/article\/bpb\/36\/11\/36_b13-00554\/_pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,3,16]],"date-time":"2021-03-16T05:30:47Z","timestamp":1615872647000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.jstage.jst.go.jp\/article\/bpb\/36\/11\/36_b13-00554\/_article"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2013]]},"references-count":29,"journal-issue":{"issue":"11","published-print":{"date-parts":[[2013]]}},"URL":"https:\/\/doi.org\/10.1248\/bpb.b13-00554","relation":{},"ISSN":["0918-6158","1347-5215"],"issn-type":[{"value":"0918-6158","type":"print"},{"value":"1347-5215","type":"electronic"}],"subject":[],"published":{"date-parts":[[2013]]}}}