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Bacteria with plasmid pE4 (<jats:italic>merR<\/jats:italic>\u2010o\/p\u2010<jats:italic>merE<\/jats:italic>) were more hypersensitive to CH<jats:sub>3<\/jats:sub>Hg(I) and Hg(II), and took up significantly more CH<jats:sub>3<\/jats:sub>Hg(I) and Hg(II), than the isogenic strain. The MerE protein encoded by pE4 was localized in the membrane cell fraction, but not in the soluble fraction. Based on these experimental results, we suggest for the first time that the <jats:italic>merE<\/jats:italic> gene is a broad mercury transporter mediating the transport of both CH<jats:sub>3<\/jats:sub>Hg(I) and Hg(II) across the bacterial membrane.<\/jats:p>","DOI":"10.1016\/j.febslet.2009.02.039","type":"journal-article","created":{"date-parts":[[2009,3,4]],"date-time":"2009-03-04T09:38:30Z","timestamp":1236159510000},"page":"1127-1131","source":"Crossref","is-referenced-by-count":64,"title":["The MerE protein encoded by transposon Tn<i>21<\/i> is a broad mercury transporter in <i>Escherichia 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