Functional Characterization of pGKT2, a 182-Kilobase Plasmid Containing the
xplAB
Genes, Which Are Involved in the Degradation of Hexahydro-1,3,5-Trinitro-1,3,5-Triazine by
Gordonia
sp. Strain KTR9
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Published:2010-10
Issue:19
Volume:76
Page:6329-6337
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ISSN:0099-2240
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Container-title:Applied and Environmental Microbiology
-
language:en
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Short-container-title:Appl Environ Microbiol
Author:
Indest Karl J.1, Jung Carina M.1, Chen Hao-Ping2, Hancock Dawn1, Florizone Christine2, Eltis Lindsay D.2, Crocker Fiona H.1
Affiliation:
1. U.S. Army Engineer Research and Development Center, Environmental Laboratory, Vicksburg, Mississippi 2. Department of Microbiology and Immunology, University of British Columbia, Vancouver, British Columbia, Canada
Abstract
ABSTRACT
Several microorganisms have been isolated that can transform hexahydro-1,3,5-trinitro-1,3,5-triazine (RDX), a cyclic nitramine explosive. To better characterize the microbial genes that facilitate this transformation, we sequenced and annotated a 182-kb plasmid, pGKT2, from the RDX-degrading strain
Gordonia
sp. KTR9. This plasmid carries
xplA
, encoding a protein sharing up to 99% amino acid sequence identity with characterized RDX-degrading cytochromes P450. Other genes that cluster with
xplA
are predicted to encode a glutamine synthase-XplB fusion protein, a second cytochrome P450, Cyp151C, and XplR, a GntR-type regulator.
Rhodococcus jostii
RHA1 expressing
xplA
from KTR9 degraded RDX but did not utilize RDX as a nitrogen source. Moreover, an
Escherichia coli
strain producing XplA degraded RDX but a strain producing Cyp151C did not. KTR9 strains cured of pGKT2 did not transform RDX. Physiological studies examining the effects of exogenous nitrogen sources on RDX degradation in strain KTR9 revealed that ammonium, nitrite, and nitrate each inhibited RDX degradation by up to 79%. Quantitative real-time PCR analysis of
glnA-xplB
,
xplA
, and
xplR
showed that transcript levels were 3.7-fold higher during growth on RDX than during growth on ammonium and that this upregulation was repressed in the presence of various inorganic nitrogen sources. Overall, the results indicate that RDX degradation by KTR9 is integrated with central nitrogen metabolism and that the uptake of RDX by bacterial cells does not require a dedicated transporter.
Publisher
American Society for Microbiology
Subject
Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology
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