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- Title
Cysteine and histidine residues are involved in Escherichia coli Tn 21 MerE methylmercury transport.
- Authors
Sone, Yuka; Uraguchi, Shimpei; Takanezawa, Yasukazu; Nakamura, Ryosuke; Pan‐Hou, Hidemitsu; Kiyono, Masako
- Abstract
Bacterial resistance to mercury compounds (mercurials) is mediated by proteins encoded by mercury resistance ( mer) operons. Six merE variants with site-directed 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( II) and CH3Hg(I). Also, the histidine residue located near to the cysteine pair was critical for Hg( II) transport, whereas the histidine residue located on the periplasmic side was critical for CH3Hg(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.
- Subjects
DRUG resistance in bacteria; MERCURY compounds; ESCHERICHIA coli; MEMBRANE proteins; CYSTEINE; METHYLMERCURY; HISTIDINE
- Publication
FEBS Open Bio, 2017, Vol 7, Issue 12, p1994
- ISSN
2211-5463
- Publication type
Article
- DOI
10.1002/2211-5463.12341