Mercury transport in bacteria

Water, Air, and Soil Pollution

Volumn 182, Issue 1-4, 2007, Pages 219-234

  Yamaguchi, Ai ^a   Tamang, Dorjee G ^a   Saier Jr , Milton H ^a  

^a UNIVERSITY OF CALIFORNIA SAN DIEGO   (United States)

Author keywords

Bacteria; Bioremediation; Detoxification; Mercury; Phylogeny; Toxicity; Transport

Indexed keywords

BACTERIA; BIOREMEDIATION; DETOXIFICATION; FISH; PROTEINS; TOXICITY;

METHYLMERCURY TRANSPORTERS; PHYLOGENY; PHYTOBIOREMEDIATION;

MERCURY (METAL);

ADENOSINE TRIPHOSPHATASE; CHAPERONE; MERCURY; MERF PROTEIN; MERP PROTEIN; MERT PROTEIN; OXIDOREDUCTASE; PROTEIN; UNCLASSIFIED DRUG;

BACTERIA; BIOREMEDIATION; DETOXIFICATION; FISH; MERCURY (METAL); PROTEINS; TOXICITY;

BIOINFORMATICS; BIOREMEDIATION; DETOXIFICATION; GENE FLOW; HEAVY METAL; MERCURY (ELEMENT); METHYLMERCURY; MICROBIAL ACTIVITY; PHYLOGENETICS; PHYTOREMEDIATION; POLLUTANT TRANSPORT; PROTEIN; TOXIC SUBSTANCE;

ARTICLE; BACTERIUM; BIOINFORMATICS; BIOREMEDIATION; DETOXIFICATION; METAL BINDING; NONHUMAN; PHYLOGENY; REDUCTION;

EID: 34248358597     PISSN: 00496979     EISSN: 15732932     Source Type: Journal    
DOI: 10.1007/s11270-007-9334-z     Document Type: Article

References (49)

1. Altschul, S. F., Madden, T. L., Schäffer, A. A., Zhang, J., Zhang, Z., Miller, W., et al. (1997). Gapped BLAST and PSI-BLAST: A new generation of protein database search programs. Nucleic Acids Research, 25, 3389-3402.
2. Barkay, T., Miller, S. M., & Summers, A. O. (2003). Bacterial mercury resistance from atoms to ecosystems. FEMS Microbiology Reviews, 27, 355-384.
3. Barkay, T., & Wagner-Dobler, I. (2005). Microbial transformations of mercury: potentials, challenges, and achievements in controlling mercury toxicity in the environment. Advances in Applied Microbiology, 57, 1-52.
4. Brejc, K., van Dijk, W. J., Klaassen, R. V., Schuurmans, M., van der Oost, J., Smit, A. B., et al. (2001). Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors. Nature, 411, 269-276.
5. 2+-contamined environments. Applied and Environmental Microbiology, 63, 2442-2445.
6. De Angelis, A. A., Howell, S. C., Nevzorov, A. A., & Opella, S. J. (2006). Structure determination of a membrane protein with two trans-membrane helices in aligned phospholipid bicelles by solid-state NMR spectroscopy. Journal of the American Chemical Society, 128, 12256-12267.
7. DeSilva, T. M., Veglia, G., & Opella, S. J. (2005). Solution structures of the reduced and Cu(I) bound forms of the first metal binding sequence of ATP7A associated with Menkes disease. Proteins, 61, 1038-1049.
8. Devereux, J., Haeberli, P., & Smithies, O. (1984). A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Research, 12, 387-395.
9. Eisler, R. (2004). Mercury hazards from gold mining to humans, plants, and animals. Reviews of Environmental Contamination and Toxicology, 181, 139-198.
10. Eisler, R. (2006). Mercury hazards to living organisms. Boca Raton, FL: CRC Taylor and Francis.
11. Goldman, L. R., Shannon, M. W., & American Academy of Pediatrics: Committee on Environmental Health (2001). Technical report: Mercury in the environment: Implications for pediatricians. Pediatrics, 108, 197-205.
12. Gray, J. S. (2002). Biomagnification in marine systems: The perspective of an ecologist. Marine Pollution Bulletin, 45, 46-52.
13. Hansen, J. C., & Gilman, A. P. (2005). Exposure of Arctic populations to methylmercury from consumption of marine food: An updated risk-benefit assessment. International Journal of Circumpolar Health, 64, 121-136.
14. Hobman, J. L., & Brown, N. L. (1996). Overexpression of MerT, the mercuric ion transport protein of transposon Tn501, and genetic selection of mercury hypersensitivity mutations. Molecular and General Genetics, 250, 129-134.
15. Howell, S. C., Mesleh, M. F., & Opella, S. J. (2005). NMR structure determination of a membrane protein with two transmembrane helices in micelles: MerF of the bacterial mercury detoxification system. Biochemistry, 44, 5196-5206.
16. Inoue, C., Kusano, T., & Silver, S. (1996). Mercuric ion uptake by Escherichia coli producing Thiobacillus ferrooxidans MerC. Bioscience, Biotechnology, and Biochemistry, 60, 1289-1292.
17. Jarup, L. (2003). Hazards of heavy metal contamination. British Medical Bulletin, 68, 167-182.
18. Kiyono, M., Uno, Y., Omura, T., & Pan-Hou, H. (2000). Role of MerT and MerP from Pseudomonas K-62 plasmid pMR26 in the transport of phenylmercury. Biological & Pharmaceutical Bulletin, 23, 279-282.
19. Kosower, E. M. (1990). Holistic approaches to receptor and channel structure and dynamics. Biochemical Society Symposia, 57, 49-64.
20. Li, W., & Godzik, A. (2006). Cd-hit: a fast program for clustering and comparing large sets of protein or nucleotide sequences. Bioinformatics, 22, 1658-1659.
21. Liebert, C. A., Watson, A. L., & Summers, A. O. (2000). The quality of merC, a module of the mer mosaic. Journal of Molecular Evolution, 51, 607-622.
22. Mahaffey, K. R. (2000). Recent advances in recognition of low-level methylmercury poisoning. Current Opinion in Neurology, 13, 699-707.
23. Miller, S. M. (1999). Bacterial detoxification of Hg(II) and organomercurials. Essays in Biochemistry, 34, 17-30.
24. Mindlin, S., Kholodii, G., Gorlenko, Z., Minakhina, S., Minakhin, L., Kalyaeva, E., et al. (2001). Mercury resistance transposons of gram-negative environmental bacteria and their classification. Research in Microbiology, 152, 811-822.
25. Morby, A. P., Hobman, J. L., & Brown, N. L. (1995). The role of cysteine residues in the transport of mercuric ions by the Tn501 MerT and MerP mercury-resistance proteins. Molecular Microbiology, 17, 25-35.
26. Nascimento, A. M., & Chartone-Souza, E. (2003). Operon mer: Bacterial resistance to mercury and potential for bioremediation of contaminated environments. Genetics and Molecular Research, 2, 92-101.
27. Osborn, A. M., Bruce, K. D., Ritchie, D. A., & Strike, P. (1996). The mercury resistance operon of the IncJ plasmid pMERPH exhibits structural and regulatory divergence from other Gram-negative mer operons. Microbiology, 142, 337-345.
28. Peters, S. E., Hobman, J. L., Strike, P., & Ritchie, D. A. (1991). Novel mercury resistance determinants carried by IncJ plasmids pMERHP and R391. Mol Gen Genet, 228, 294-299.
29. Qian, H., Sahlman, L., Eriksson, P.-O., Hambraeus, C., Edlund, U., & Sethson, I. (1998). NMR solution structure of the oxidized form of MerP, a mercuric ion binding protein involved in bacterial mercuric ion resistance. Biochemistry, 37, 9316-9322.
30. Rossy, E., Seneque, O., Lascoux, D., Lemaire, D., Crouzy, S., Delangle, P., et al. (2004). Is the cytoplasmic loop of MerT, the mercuric ion transport protein, involved in mercury transfer to the mercuric reductase? FEBS Letters, 575, 86-90.
31. Sahlman, L., Wong, W., & Powlowski, J. (1997). A mercuric ion uptake role for the integral inner membrane protein, MerC, involved in bacterial mercuric ion resistance. Journal of Biological Chemistry, 272, 29518-29526.
32. Saier, M. H., Jr. (1994). Computer-aided analyses of transport protein sequences: Gleaning evidence concerning function, structure, biogenesis, and evolution. Microbiological Reviews, 58, 71-93.
33. Saier, M. H., Jr. (2003a). Tracing pathways of transport protein evolution. Molecular Microbiology, 48, 1145-1156.
34. Saier, M. H., Jr. (2003b). Answering fundamental questions in biology with bioinformatics. ASM News, 69, 175-181.
35. Sasaki, Y., Hayakawa, T., Inoue, C., Miyazaki, A., Silver, S., & Kusano, T. (2006). Generation of mercury-hyperaccumulating plants through transgenic expression of the bacterial mercury membrane transport protein MerC. Transgenic Research, 15, 615-625.
36. Schaefer, J. K., Yagi, J., Reinfelder, J. R., Cardona, T., Ellickson, K. M., Tel-Or, S., et al. (2004). Role of the bacterial organomercury lyase (MerB) in controlling methylmercury accumulation in mercury-contaminated natural waters. Environmental Science & Technology, 38, 4304-4311.
37. Serre, L., Rossy, E., Pebay-Peyroula, E., Cohen-Addad, C., & Covès, J. (2004). Crystal structure of the oxidized form of the periplasmic mercury-binding protein MerP from Ralstonia metallidurans CH34. Journal of Molecular Biology, 339, 161-171.
38. Silver, S., & Phung, L. T. (1996). Bacterial heavy metal resistance: New surprises. Annual Review of Microbiology, 50, 753-789.
39. Steele, R. A., & Opella, S. J. (1997). Structures of the reduced and mercury-bound forms of MerP, the periplasmic protein from the bacterial mercury detoxification system. Biochemistry, 36, 6885-6895.
40. Thompson, J. D., Gibson, T. J., Plewniak, F., Jeanmougin, F., & Higgins, D. G. (1997). The CLUSTAL X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Research, 25, 4876-4882.
41. Uno, Y., Kiyono, M., Tezuka, T., & Pan-Hou, H. (1997). Phenylmercury transport mediated by merT-merP genes of Pseudomonas K-62 plasmid pMR26. Biological & Pharmaceutical Bulletin, 20, 107-109.
42. Velasco, A., Acebo, P., Flores, N., & Perera, J. (1999). The mer operon of the acidophilic bacterium Thiobacillus T3.2 diverges from its Thiobacillus ferrooxidans counterpart. Extremophiles, 3, 35-43.
43. von Heijne, G., & Gavel, Y. (1988). Topogenic signals in integral membrane proteins. European Journal of Biochemistry, 174, 671-678.
44. Wilson, J. R., Leang, C., Morby, A. P., Hobman, J. L., & Brown, N. L. (2000). MerF is a mercury transport protein: Different structures but a common mechanism for mercuric ion transporters? FEBS Letters, 472, 78-82.
45. Wimmer, R., Herrmann, T., Solioz, M., & Wuthrich, K. (1999). NMR structure and metal interactions of the CopZ copper chaperone. Journal of Biological Chemistry, 274, 22597-22603.
46. Yeo, C. C., Tham, J. M., Kwong, S. M., Yiin, S., & Poh, C. L. (1998). Tn5563, a transposon encoding putative mercuric ion transport proteins located on plasmid pRA2 of Pseudomonas alcaligenes. FEMS Microbiology Letters, 165, 253-260.
47. Zhai, Y., & Saier, M. H., Jr. (2001a). A web-based program (WHAT) for the simultaneous prediction of hydropathy, amphipathicity, secondary structure and transmembrane topology for a single protein sequence. Journal of Molecular Microbiology and Biotechnology, 3, 501-502.
48. Zhai, Y., & Saier, M. H., Jr. (2001b). A web-based program for the prediction of average hydropathy, average amphipathicity and average similarity of multiply aligned homologous proteins. Journal of Molecular Microbiology and Biotechnology, 3, 285-286.
49. Zhai, Y., Tchieu, J., & Saier, M. H., Jr. (2002). A web-based tree view (TV) program for the visualization of phylogenetic trees. Journal of Molecular Microbiology and Biotechnology, 4, 69-70.