Involvement of Aromatic Amino Acids in Phenylmercury Transport by MerT Protein
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- Nagata Takeshi
- Faculty of Pharmaceutical Sciences, Setsunan University
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- Kiyono Masako
- Faculty of Pharmaceutical Sciences, Setsunan University
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- Pan-Hou Hidemitsu
- Faculty of Pharmaceutical Sciences, Setsunan University
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Abstract
To investigate the role of aromatic amino acids of MerT protein in phenylmercury transport, two merT variants (pMRTm1P and pMRTm2P) with specific site-directed mutations were constructed and examined their effects on C6H5Hg+-transport. Substitution of Phe-36 and Trp-40 residues located on the periplasmic loop of MerT in turn with Ala and Val, respectively, did not affect the Hg2+-uptake, but caused a significant reduction in the C6H5Hg+-uptake by bacterial cells with intact merT gene. Introduction of specific mutations changing Phe-108, 114, 115 to Ala, and Tyr-110, 116 to Ser in the C-terminal region of the third transmembrane of MerT also caused large reduction in the uptake of C6H5Hg+, but had no effect on the Hg2+-uptake. In addition, both mutations caused a significant reduction in the hypersensitivity to C6H5Hg+, but without affecting the Hg2+-hypersensitive phenotype. Together these results suggest that the aromatic amino acids of MerT protein may play an important role in the transport of C6H5Hg+ across the cell membrane. <br>
Journal
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- Journal of Health Science
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Journal of Health Science 52 (4), 475-477, 2006
The Pharmaceutical Society of Japan
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Details
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- CRID
- 1390282679474175232
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- NII Article ID
- 110006251407
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- NII Book ID
- AA11316464
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- ISSN
- 13475207
- 13449702
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- NDL BIB ID
- 7991401
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed