Rhizosphere competitiveness of trichloroethylene-degrading, poplar-colonizing recombinant bacteria

Appl Environ Microbiol. 2000 Nov;66(11):4673-8. doi: 10.1128/AEM.66.11.4673-4678.2000.

Abstract

Indigenous bacteria from poplar tree (Populus canadensis var. eugenei 'Imperial Carolina') and southern California shrub rhizospheres, as well as two tree-colonizing Rhizobium strains (ATCC 10320 and ATCC 35645), were engineered to express constitutively and stably toluene o-monooxygenase (TOM) from Burkholderia cepacia G4 by integrating the tom locus into the chromosome. The poplar and Rhizobium recombinant bacteria degraded trichloroethylene at a rate of 0.8 to 2.1 nmol/min/mg of protein and were competitive against the unengineered hosts in wheat and barley rhizospheres for 1 month (colonization occurred at a level of 1.0 x 10(5) to 23 x 10(5) CFU/cm of root). In addition, six of these recombinants colonized poplar roots stably and competitively with populations as large as 79% +/- 12% of all rhizosphere bacteria after 28 days (0.2 x 10(5) to 31 x 10(5) CFU/cm of root). Furthermore, five of the most competitive poplar recombinants (e.g., Pb3-1 and Pb5-1, which were identified as Pseudomonas sp. strain PsK recombinants) retained the ability to express TOM for 29 days as 100% +/- 0% of the recombinants detected in the poplar rhizosphere expressed TOM constitutively.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Biodegradation, Environmental
  • Hordeum / microbiology
  • Mixed Function Oxygenases / genetics
  • Mixed Function Oxygenases / metabolism
  • Plant Roots / microbiology*
  • Pseudomonas / genetics
  • Pseudomonas / growth & development*
  • Pseudomonas / metabolism
  • Recombination, Genetic*
  • Rhizobium / growth & development
  • Rhizobium / metabolism
  • Trees / growth & development
  • Trees / microbiology*
  • Trichloroethylene / metabolism*
  • Triticum / microbiology

Substances

  • Trichloroethylene
  • Mixed Function Oxygenases
  • toluene ortho-monooxygenase