Skip to main content

Bacterial Mercury Resistance Proteins

  • Reference work entry
Encyclopedia of Metalloproteins

Synonyms

Microbial toxic mercury resistance; Proteins with mercury as “natural” substrate

Definition

Bacteria carry out chemical transformations of mercury compounds. Often these transformations result from bacterial resistance systems to inorganic mercury (Hg2+) and to organomercurials (such as methylmercury and phenylmercury). There are four types of mercury-specific proteins: detoxifying enzymes producing less toxic products, membrane transport proteins that bring Hg2+ into the cells to be detoxified, mercury-binding proteins at the outer cell surface, and DNA-binding transcriptional regulatory proteins governing mRNA synthesis (Barkay et al. 2003; Silver and Phung 2005; Silver and Hobman 2007).

Mercury Resistance (the mer Operon)

The genes for bacterial mercury resistance are clustered in a “meroperon” of contiguous genes that are regulated together and are found widely on the plasmids and the chromosomes of both gram-positive and gram-negative bacteria. The number of genes (and...

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 799.99
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Hardcover Book
USD 549.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

References

  • Barkay T, Miller SM, Summers AO (2003) Bacterial mercury resistance from atoms to ecosystems. FEMS Microbiol Rev 27:355–384

    Article  PubMed  CAS  Google Scholar 

  • Brown NL, Shih Y-C, Leang C, Glendinning KJ, Hobman JL, Wilson JR (2002) Mercury transport and resistance. Biochem Soc Trans 30:715–718

    Article  PubMed  CAS  Google Scholar 

  • Brown NL, Stoyanov JV, Kidd SP, Hobman JL (2003) The MerR family of transcriptional regulators. FEMS Microbiol Rev 27:145–163

    Article  PubMed  CAS  Google Scholar 

  • Changela A, Chen K, Xue Y, Holschen J, Outten CE, O`Halloran TV, Mondragon A (2003) Molecular basis of metal-ion selectivity and zeptomolar sensitivity by CueR. Science 301:1383–1387

    Article  PubMed  CAS  Google Scholar 

  • Chen CY, Hsieh JL, Silver S, Endo G, Huang CC (2008) Interactions between two MerR regulators and three operator/promoter regions in the mercury resistance module of Bacillus megaterium. Biosci Biotechnol Biochem 72:2403–2410

    Article  PubMed  CAS  Google Scholar 

  • Guo H-B, Johs A, Parks JM, Olliff L, Miller SM, Summers AO, Liang L, Smith JC (2010) Structure and conformational dynamics of the metalloregulator MerR upon binding of Hg(II). J Mol Biol 398:555–568

    Article  PubMed  CAS  Google Scholar 

  • Howell SC, Mesleh MF, Opella SJ (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

    Article  PubMed  CAS  Google Scholar 

  • Kaisa M, Hakkila KM, Nikander PA, Junttila SM, Lamminmäki UJ, Virta MP (2011) Cd-specific mutants of mercury-sensing regulatory protein MerR, generated by directed evolution. Appl Environ Microbiol 77:6215–6224

    Article  CAS  Google Scholar 

  • Lafrance-Vanasse J, Lefebvre M, Di Lello P, Sygusch J, Omichinski JG (2009) Crystal structures of the organomercurial lyase MerB in its free and mercury-bound forms. J Biol Chem 284:938–944

    Article  PubMed  CAS  Google Scholar 

  • Ledwidge R, Patel B, Dong A, Fiedler D, Falkowski M, Zelikova J, Summers AO, Pai EF, Miller SM (2005) NmerA, the metal binding domain of mercuric ion reductase, removes Hg2+ from proteins, delivers it to the catalytic core, and protects cells under glutathione-depleted conditions. Biochemistry 44:11402–11416

    Article  PubMed  CAS  Google Scholar 

  • Miller SM (2007) Cleaving C-Hg bonds: two thiolates are better than one. Nat Chem Biol 3:537–538

    Article  PubMed  CAS  Google Scholar 

  • Parks JM, Guo H, Momany C, Liang L, Miller SM, Summers AO, Smith JC (2009) Mechanism of Hg−C protonolysis in the organomercurial lyase MerB. J Am Chem Soc 131:13278–13285

    Article  PubMed  CAS  Google Scholar 

  • Serre L, Rossy E, Pebay-Peyroula E, Cohen-Addad C, Coves J (2004) Crystal structure of the oxidized form of the periplasmic mercury-binding protein MerP from Ralstonia metallidurans CH34. J Mol Biol 339:161–171

    Article  PubMed  CAS  Google Scholar 

  • Silver S, Hobman J (2007) Mercury microbiology: resistance systems, environmental aspects, methylation and human health. In: Nies DH, Silver S (eds) Molecular microbiology of heavy metals. Springer, Heidelberg, pp 357–370

    Chapter  Google Scholar 

  • Silver S, Phung LT (2005) A bacterial view of the Periodic Table: genes and proteins for toxic inorganic ions. J Ind Microbiol Biotechnol 32:587–605

    Article  PubMed  CAS  Google Scholar 

  • Smith T, Pitts K, McGarvey JA, Summers AO (1998) Bacterial oxidation of mercury metal vapor, Hg(0). Appl Environ Microbiol 64:1328–1332

    PubMed  CAS  Google Scholar 

  • Steele RA, Opella SJ (1997) Structures of the reduced and mercury-bound forms of MerP, the periplasmic protein from the bacterial mercury detoxification system. Biochemistry 36:6885–6895

    Article  PubMed  CAS  Google Scholar 

  • Utschig LM, Bryson JW, O’Halloran TV (1995) Mercury-199 NMR of the metal receptor site in MerR and its protein-DNA complex. Science 268:380–385

    Article  PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Simon Silver .

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 2013 Springer Science+Business Media New York

About this entry

Cite this entry

Silver, S., Phung, L.T. (2013). Bacterial Mercury Resistance Proteins. In: Kretsinger, R.H., Uversky, V.N., Permyakov, E.A. (eds) Encyclopedia of Metalloproteins. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-1533-6_312

Download citation

Publish with us

Policies and ethics