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...
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Barkay T, Miller SM, Summers AO (2003) Bacterial mercury resistance from atoms to ecosystems. FEMS Microbiol Rev 27:355–384
Brown NL, Shih Y-C, Leang C, Glendinning KJ, Hobman JL, Wilson JR (2002) Mercury transport and resistance. Biochem Soc Trans 30:715–718
Brown NL, Stoyanov JV, Kidd SP, Hobman JL (2003) The MerR family of transcriptional regulators. FEMS Microbiol Rev 27:145–163
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
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
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
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
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
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
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
Miller SM (2007) Cleaving C-Hg bonds: two thiolates are better than one. Nat Chem Biol 3:537–538
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
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
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
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
Smith T, Pitts K, McGarvey JA, Summers AO (1998) Bacterial oxidation of mercury metal vapor, Hg(0). Appl Environ Microbiol 64:1328–1332
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
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
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights 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
DOI: https://doi.org/10.1007/978-1-4614-1533-6_312
Publisher Name: Springer, New York, NY
Print ISBN: 978-1-4614-1532-9
Online ISBN: 978-1-4614-1533-6
eBook Packages: Biomedical and Life SciencesReference Module Biomedical and Life Sciences