Cysteine and histidine residues are involved in Escherichia coli Tn21 MerE methylmercury transport.
Cysteine and histidine residues are involved in Escherichia coli Tn21 MerE methylmercury transport.
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DOI：
10.1002/2211-5463.12341
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发表时间：
2017-12
期刊：
影响因子：
2.6
通讯作者：
Kiyono M
中科院分区：
文献类型：
--
作者：
Sone Y;Uraguchi S;Takanezawa Y;Nakamura R;Pan-Hou H;Kiyono M
细菌对汞化合物（汞剂）的抗性是由耐汞操纵子编码的蛋白质介导的。构建了6个具有定点突变的merE变体，以研究MerE蛋白中半胱氨酸和组氨酸残基在汞转运过程中的作用。通过比较具有完整和/或变异MerE的细胞对汞的摄取，我们发现第一跨膜结构域中的半胱氨酸对对于Hg（II）和CH 3 Hg（I）的转运至关重要。此外，位于半胱氨酸对附近的组氨酸残基是至关重要的Hg（II）的运输，而位于周质侧的组氨酸残基是至关重要的CH 3 Hg（I）的运输。因此，由MerE介导的增强的汞吸收可能是用于环境中汞的生物修复的新生物质的设计的一个有前途的策略。
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 3Hg(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 3Hg(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.
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影响因子：
3.5
作者：
HASHIMOTOGOTOH, T;MIZUNO, T;NAKAGAWA, M
通讯作者：
NAKAGAWA, M
影响因子：
56.9
作者：
Melnick, Jonathan G.;Parkin, Gerard
通讯作者：
Parkin, Gerard
影响因子：
3.9
作者：
Brown, NL;Shih, YC;Wilson, JR
通讯作者：
Wilson, JR
DOI：
10.1073/pnas.84.10.3112
发表时间：
1987-05-01
影响因子：
11.1
作者：
GRIFFIN, HG;FOSTER, TJ;MISRA, TK
通讯作者：
MISRA, TK
影响因子：
3.5
作者：
Wilson, JR;Leang, C;Brown, NL
通讯作者：
Brown, NL