Advanced search
Publication Cover
Bioscience, Biotechnology, and Biochemistry Volume 69, 2005 - Issue 7
Journal homepage
200
Views
32
CrossRef citations to date
0
Altmetric
Original Articles

Functional Dissection of a Mercuric Ion Transporter, MerC, from Acidithiobacillus ferrooxidans

Yoshito SASAKIGraduate School of Life Sciences, Tohoku University
,
Takahiro MINAKAWAGraduate School of Life Sciences, Tohoku University
,
Atushi MIYAZAKIGraduate School of Life Sciences, Tohoku University
,
Simon SILVERDepartment of Microbiology and Immunology, M/C 790, University of Illinois
&
Tomonobu KUSANOGraduate School of Life Sciences, Tohoku University
Pages 1394-1402 | Received 06 Apr 2005, Accepted 26 Apr 2005, Published online: 22 May 2014

  • 1) Barkay, T., Miller, S. M., and Summers, A. O., Bacterial mercury resistance from atoms to ecosystems. FEMS Microbiol. Rev., 27, 355–384 (2003).
  • 2) Brown, N. L., Shih, Y. C., Leang, C., Glendinning, K. J., Hobman, J. L., and Wilson, J. R., Mercury transport and resistance. Biochem. Soc. Trans., 30, 715–718 (2002).
  • 3) Brown, N. L., Misra, T. K., Winnie, J. N., Schmidt, A., Seiff, M., and Silver, S., The nucleotide sequence of the mercuric resistance operons of plasmid R100 and transposon Tn501: further evidence for mer genes which enhance the activity of the mercuric ion detoxification system. Mol. Gen. Genet., 202, 143–151 (1986).
  • 4) Misra, T. K., Brown, N. L., Fritzinger, D. C., Pridmore, R. D., Barnes, W. M., Haberstroh, L., and Silver, S., Mercuric ion-resistance operons of plasmid R100 and transposon Tn501: the beginning of the operon including the regulatory region and the first two structural genes. Proc. Natl. Acad. Sci. U.S.A., 81, 5975–5979 (1984).
  • 5) Misra, T. K., Brown, N. L., Haberstroh, L., Schmidt, A., Goddette, D., and Silver, S., Mercuric reductase structural genes from plasmid R100 and transposon Tn501: functional domains of the enzyme. Gene, 34, 253–262 (1985).
  • 6) Nucifora, G., Chu, L., Silver, S., and Misra, T. K., Mercury operon regulation by the merR gene of the organomercurial resistance system of plasmid pDU1358. J. Bacteriol., 171, 4241–4247 (1989).
  • 7) Silver, S., and Misra, T. K., Plasmid-mediated heavy metal determinant mer resistance. Annu. Rev. Microbiol., 42, 717–743 (1988).
  • 8) Mukhopadhyay, D., Yu, H. R., Nucifora, G., and Misra, T. K., Purification and functional characterization of MerD: a coregulator of the mercury resistance operon in gram-negative bacteria. J. Biol. Chem., 266, 18538–18542 (1991).
  • 9) Hamlett, N. V., Landale, E. C., Davis, B. H., and Summers, A. O., Roles of the Tn21 merT, merP, and merC gene products in mercury resistance and mercury binding. J. Bacteriol., 174, 6377–6385 (1992).
  • 10) Inoue, C., Sugawara, K., and Kusano, T., The merR regulatory gene in Thiobacillus ferrooxidans is spaced apart from the mer structural genes. Mol. Microbiol., 5, 2707–2718 (1991).
  • 11) Rawlings, D. E., and Kusano, T., Molecular genetics of Thiobacillus ferrooxidans. Microbiol. Rev., 158, 39–55 (1994).
  • 12) Kusano, T., Ji, G., Inoue, C., and Silver, S., Constitutive synthesis of a transport function encoded by the Thiobacillus ferrooxidans merC gene cloned in Escherichia coli. J. Bacteriol., 172, 2688–2692 (1990).
  • 13) Inoue, C., Kusano, T., and Silver, S., Mercuric ion uptake by Escherichia coli cells producing Thiobacillus ferrooxidans MerC. Biosci. Biotechnol. Biochem., 60, 1289–1292 (1996).
  • 14) Sahlman, L., Wong, W., and Powlowski, J., A mercuric ion uptake role for the integral inner membrane protein, MerC, involved in bacterial mercuric ion resistance. J. Biol. Chem., 272, 29518–29526 (1997).
  • 15) Sahlman, L., Hagglof, E. M., and Powlowski, J., Roles of the four cysteine residues in the function of the integral inner membrane Hg2+-binding protein, MerC. Biochem. Biophys. Res. Commun., 255, 307–311 (1999).
  • 16) Wilson, J. R., Leang, C., Morby, A. P., Hobman, J. L., and Brown, N. L., MerF is a mercury transport protein: different structures but a common mechanism for mercuric ion transporters? FEBS Lett., 472, 78–82 (2000).
  • 17) Manoil, C., and Beckwith, J., TnphoA: a transposon probe for protein export signals. Proc. Natl. Acad. Sci. U.S.A., 82, 8129–8133 (1985).
  • 18) Ehrmann, M., Bolek, P., Mondigler, M., Boyd, D., and Lange, R., TnTIN and TnTAP: mini-transposons for site-specific proteolysis in vivo. Proc. Natl. Acad. Sci. U.S.A., 94, 13111–13115 (1997).
  • 19) Gutierrez, C., and Devedjian, J. C., A plasmid facilitating in vitro construction of phoA gene fusions in Escherichia coli. Nucl. Acids Res., 17, 3999 (1989).
  • 20) Shiratori, T., Inoue, C., Sugawara, K., Kusano, T., and Kitagawa, Y., Cloning and expression of Thiobaccilus ferrooxidans mercury ion resistance genes in Escherichia coli. J. Bacteriol., 171, 3458–3464 (1989).
  • 21) Sambrook, J., and Russell, D. W., Molecular cloning: a laboratory manual, Third ed., Cold Spring Harbor Laboratory, Cold Spring Harbor, New York, A8.45 (2001).
  • 22) Guzman, L. M., Belin, D., Carson, M. J., and Beckwith, J., Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J. Bacteriol., 177, 4121–4130 (1995).
  • 23) Michaelis, S., Inouye, H., Oliver, D., and Beckwith, J., Mutations that alter the signal sequence of alkaline phosphatase in Escherichia coli. J. Bacteriol., 154, 366–374 (1983).
  • 24) Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K., and Pease, L. R., Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene, 77, 51–59 (1989).
  • 25) Melchers, K., Schuhmacher, A., Buhmann, A., Weitzenegger, T., Belin, D., Grau, S., and Ehrmann, M., Membrane topology of CadA homologous P-type ATPase of Helicobacter pylori as determined by expression of phoA fusions in Escherichia coli and the positive inside rule. Res. Microbiol., 150, 507–520 (1999).
  • 26) Williams, L. E., Pittman, J. K., and Hall, J. L., Emerging mechanisms for heavy metal transport in plants. Biochim. Biophys. Acta, 1465, 104–126 (2000).
  • 27) Morby, A. P., Hobman, J. L., and Brown, N. L., The role of cysteine residues in the transport of mercuric ions by the Tn501 MerT and MerP mercury-resistance proteins. Mol. Microbiol., 17, 25–35 (1995).
  • 28) Solioz, M., and Vulpe, C., CPx-type ATPases: a class of P-type ATPases that pump heavy metals. Trends Biochem. Sci., 21, 237–241 (1996).
  • 29) Gitschier, J., Moffat, B., Reilly, D., Wood, W. I., and Fairbrother, W. J., Solution structure of the fourth metal-binding domain from the Menkes copper-transporting ATPase. Nat. Struct. Biol., 5, 47–54 (1998).
  • 30) Rossy, E., Champier, L., Bersch, B., Brutscher, B., Blackledge, M., and Coves, J., Biophysical characterization of the MerP-like amino-terminal extension of the mercuric reductase from Ralstonia metallidurans CH34. J. Biol. Inorg. Chem., 9, 49–58 (2004).
  • 31) Rossy, E., Seneque, O., Lascoux, D., Lemaire, D., Crouzy, S., Delangle, P., and Coves, J., Is the cytoplasmic loop of MerT, the mercuric ion transport protein, involved in mercury transfer to the mercuric reductase? FEBS Lett., 575, 86–90 (2004).
  • 32) Liebert, C. A., Watson, A. L., and Summers, A. O., The quality of merC, a module of the mer mosaic. J. Mol. Evol., 51, 607–622 (2000).

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Order Reprints Request Corporate Permissions

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

Request Academic Permissions

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.

Related research

People also read lists articles that other readers of this article have read.

Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.

Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.