{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,6]],"date-time":"2025-11-06T12:16:05Z","timestamp":1762431365887},"reference-count":28,"publisher":"Wiley","issue":"12","license":[{"start":{"date-parts":[[2017,11,15]],"date-time":"2017-11-15T00:00:00Z","timestamp":1510704000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["JP15K18907","JP15H02839"],"award-info":[{"award-number":["JP15K18907","JP15H02839"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["FEBS Open Bio"],"published-print":{"date-parts":[[2017,12]]},"abstract":"<jats:p>Bacterial resistance to mercury compounds (mercurials) is mediated by proteins encoded by mercury resistance (<jats:italic>mer<\/jats:italic>) operons. Six <jats:italic>merE<\/jats:italic> variants with site\u2010directed mutations were constructed to investigate the roles of the cysteine and histidine residues in MerE protein during mercurial transport. By comparison of mercurial uptake by the cell with intact and\/or variant MerE, we showed that the cysteine pair in the first transmembrane domain was critical for the transport of both Hg(<jats:styled-content style=\"fixed-case\">II<\/jats:styled-content>) and <jats:styled-content style=\"fixed-case\">CH<\/jats:styled-content><jats:sub>3<\/jats:sub>Hg(I). Also, the histidine residue located near to the cysteine pair was critical for Hg(<jats:styled-content style=\"fixed-case\">II<\/jats:styled-content>) transport, whereas the histidine residue located on the periplasmic side was critical for <jats:styled-content style=\"fixed-case\">CH<\/jats:styled-content><jats:sub>3<\/jats:sub>Hg(I) transport. Thus, enhanced mercurial uptake mediated by MerE may be a promising strategy for the design of new biomass for use in the bioremediation of mercurials in the environment.<\/jats:p>","DOI":"10.1002\/2211-5463.12341","type":"journal-article","created":{"date-parts":[[2017,11,6]],"date-time":"2017-11-06T15:32:35Z","timestamp":1509982355000},"page":"1994-1999","update-policy":"http:\/\/dx.doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":12,"title":["Cysteine and histidine residues are involved in <i>Escherichia coli<\/i> Tn<i>21<\/i> MerE methylmercury transport"],"prefix":"10.1002","volume":"7","author":[{"given":"Yuka","family":"Sone","sequence":"first","affiliation":[{"name":"Department of Public Health School of Pharmacy Kitasato University Tokyo Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shimpei","family":"Uraguchi","sequence":"additional","affiliation":[{"name":"Department of Public Health School of Pharmacy Kitasato 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