| Title: | Bacterial mercury resistance from atoms to ecosystems |
| Author(s): | Barkay T; Miller SM; Summers AO; |
| Address: | "Department of Biochemistry and Microbiology, Cook College, Rutgers University, New Brunswick, NJ, USA. barkay@aesop.rutgers.edu" |
| DOI: | 10.1016/S0168-6445(03)00046-9 |
| ISSN/ISBN: | 0168-6445 (Print) 0168-6445 (Linking) |
| 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" |
| Keywords: | "Amino Acid Sequence Drug Resistance, Bacterial/*genetics Ecosystem Genes, Bacterial/genetics Gram-Negative Bacteria/enzymology/genetics Industrial Waste Ion Transport Mercury/*metabolism/pharmacology/toxicity Mercury Compounds/analysis/metabolism Models, ;" |
| Notes: | "MedlineBarkay, Tamar Miller, Susan M Summers, Anne O eng Review England 2003/06/28 FEMS Microbiol Rev. 2003 Jun; 27(2-3):355-84. doi: 10.1016/S0168-6445(03)00046-9" |
