Identification and characterization of the arsenite methyltransferase from a protozoan, Tetrahymena pyriformis

Aquat Toxicol. 2014 Apr:149:50-7. doi: 10.1016/j.aquatox.2014.01.028. Epub 2014 Feb 8.

Abstract

Arsenic (As) methylation in aquatic microbes plays a major role in the biogeochemistry of As. Protozoa, especially the free-living freshwater species, are important players in aquatic ecological health. In this study, an arsenite (As(III)) methyltransferase, TpyArsM, was identified and characterized in a free-living protozoan, Tetrahymena pyriformis. In order to confirm its function, TpyarsM gene was knocked-out in Tetrahymena and was also heterologously expressed in hypersensitive E. coli; these events resulted in expected decreases in As tolerance and methylation ability, respectively. In-vitro tests revealed that purified TpyArsM protein methylated inorganic As to mono- and di- methylarsenate, and also had the novel property of producing trimethylarsenite (TMA(III)) and dimethylarsine (Me2AsH) gases. This new methyltransferase gene, identified in a species near the base of the food web, has enriched our knowledge of As methyltransferases and has great potential for bioremediation of As-contaminated environments.

Keywords: Arsenic; Heavy metal; Methylarsine; Methyltransferase; Protozoan; Tetrahymena pyriformis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arsenic / chemistry
  • Arsenic / metabolism*
  • Escherichia coli / genetics
  • Gene Expression Regulation, Enzymologic*
  • Gene Knockout Techniques
  • Inhibitory Concentration 50
  • Methylation
  • Methyltransferases / genetics*
  • Methyltransferases / metabolism*
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Tetrahymena pyriformis / enzymology*
  • Tetrahymena pyriformis / genetics*
  • Volatilization

Substances

  • Recombinant Proteins
  • Methyltransferases
  • arsenite methyltransferase
  • Arsenic