Cited by 1,054Mercury impact and mitigation studiesBacterial Genetics and BiotechnologyMicrobial metabolism and enzyme function

Bacterial mercury resistance from atoms to ecosystems

Open access
Barkay, Tamar, Miller, Susan M., Summers, Anne O.·2003·FEMS Microbiology Reviews

Abstract

Bacterial resistance to inorganic and organic mercury compounds (HgR) is one of the most widely observed phenotypes in eubacteria. Loci conferring HgR in Gram-positive or Gram-negative bacteria typically have at minimum a mercuric reductase enzyme (MerA) that reduces reactive ionic Hg(II) to volatile, relatively inert, monoatomic Hg(0) vapor and a membrane-bound protein (MerT) for uptake of Hg(II) arranged in an operon under control of MerR, a novel metal-responsive regulator. Many HgR loci encode an additional enzyme, MerB, that degrades organomercurials by protonolysis, and one or more additional proteins apparently involved in transport. Genes conferring HgR occur on chromosomes, plasmids, and transposons and their operon arrangements can be quite diverse, frequently involving duplications of the above noted structural genes, several of which are modular themselves. How this very mobile and plastic suite of proteins protects host cells from this pervasive toxic metal, what roles it has in the biogeochemical cycling of Hg, and how it has been employed in ameliorating environmental contamination are the subjects of this review.

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Crossref · 10.1016/s0168-6445(03)00046-9

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  • Hg(II) is transported into the cell via the MerT transporter protein and detoxified by reduction to relatively nontoxic volatile elemental mercury by an intracellular mercuric reductase (MerA).

    “Here, Hg(II) is transported into the cell via the MerT transporter protein, and detoxi¢ed by reduction to relatively nontoxic volatile elemental mercury by an intracellular mercuric reductase (MerA).”

    From Microbial reduction of metals and radionuclides (2003) · cites this paper as [5]

  • Bacterial cells exposed to Hg2+ sense this metal and mount a transcriptional response within minutes.

    “bacterial cells exposed to Hg2+ sense this metal and mount a transcriptional response within minutes.209”
  • Despite its extremely high affinity for sulfur-containing ligands, Hg2+ is surprisingly mobile.

    “Despite this extremely high affinity, Hg2+ is surprisingly mobile”

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Research works printed but not linked: 6

  1. [40]40. National Research Council (2000) Toxicological E¡ects of Methyl- mercury. National Academy Press, Washington, DC.
  2. [108]108. Kim, K.-H., Hanson, P.J., Barnett, M.O. and Lindberg, S.E. (1997) Biogeochemistry of mercury in the air-soil-plant system. In: Mer- cury and its E¡ects on Environment and Biology, 1st edn., Vol. 34
  3. [144]144. Wright, J.G. (1991) Spectroscopic and chemical characterization of the mercury receptor site in the transcriptional activator MerR. Ph.D. Dissertation. Northwestern University, Evanston, IL.
  4. [223]223. Miller, S.M. (1999) Construction of separate expression vectors for the catalytic core and the N-terminal metal binding domain of Tn501 mercuric ion reductase. In: Flavins and Flavoproteins 1999 (Ghisla, S., Kroneck, P., Macheroux, P. and Sund, H., Eds.), pp. 863^870. Rudolf Weber Agency for Scienti¢c Publications, Berlin.
  5. [233]233. Newton, G.L. and Fahey, R.C. (1989) Glutathione in procaryotes. In: Glutathione: Metabolism and Physiological Functions (Vin ‹a, J., Ed.), pp. 69^77. CRC Press, Boca Raton, FL.
  6. [246]246. Laddaga, R.A., Chu, L., Misra, T.K. and Silver, S. (1987) Nucleo- tide sequence and expression of the mercurial-resistance operon from Staphylococcus aureus plasmid pI258. Proc. Natl. Acad. Sci. USA 84, 5106^5110.

Cited by

Authors
Barkay, T., Miller, S. M., & Summers, A. O.
Affiliations
  • Rutgers, The State University of New Jersey (US)
  • University of California, San Francisco (US)
  • University of Georgia (US)
Corresponding author
Summers, Anne O.
Venue
FEMS Microbiology Reviews
Published
2003-06
Volume
27
Issue
2-3
Pages
355-384
ISSN
  • 0168-6445 (ISSN-L)
  • 1574-6976
OpenAlex
W2161714667
Cited by
1,054
References
295
Citations by year
2026: 31 · 2025: 30 · 2024: 47 · 2023: 44 · 2022: 56 · 2021: 58 · 2020: 44 · 2019: 63 · 2018: 43 · 2017: 50 · 2016: 53 · 2015: 55 · 2014: 55 · 2013: 69 · 2012: 57
FWCI
3.87
Type
journal article
Language
en
Open access
Locations
  • FEMS Microbiology Reviews (publishedVersion)
  • PubMed (publishedVersion)
  • Rutgers University Community Repository (Rutgers University) (submittedVersion)
Topics
  • Physical Sciences › Environmental Science › Health, Toxicology and Mutagenesis › Mercury impact and mitigation studies
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial metabolism and enzyme function
Keywords
mercuric reductase, MERA, MerB, MerR, MERT, plasmids, transposable elements, gene duplication, mercury cycling, mercury contamination
MeSH terms
Amino Acid Sequence, Genes, Bacterial, Gram-Negative Bacteria, Industrial Waste, Mercury, Models, Biological, Models, Genetic, Molecular Sequence Data, Oxidoreductases, Sequence Alignment, Ion Transport, Mercury Compounds, Ecosystem, Drug Resistance, Bacterial

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