Open AccessCysteine and histidine residues are involved in Escherichia coli Tn 21 MerE methylmercury transport
Author(s) -
Sone Yuka,
Uraguchi Shimpei,
Takanezawa Yasukazu,
Nakamura Ryosuke,
PanHou Hidemitsu,
Kiyono Masako
Publication year - 2017
Publication title -
febs open bio
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.718
H-Index - 31
ISSN - 2211-5463
DOI - 10.1002/2211-5463.12341
Subject(s) - histidine , cysteine , periplasmic space , chemistry , residue (chemistry) , biochemistry , escherichia coli , transmembrane domain , transmembrane protein , transport protein , methylmercury , amino acid , gene , enzyme , organic chemistry , receptor , selenium
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 CH 3 Hg(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 CH 3 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.