This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental material
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Andeer, P. F.
Right arrow Articles by Strand, S. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Andeer, P. F.
Right arrow Articles by Strand, S. E.
Agricola
Right arrow Articles by Andeer, P. F.
Right arrow Articles by Strand, S. E.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, May 2009, p. 3258-3262, Vol. 75, No. 10
0099-2240/09/$08.00+0     doi:10.1128/AEM.02396-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Lateral Transfer of Genes for Hexahydro-1,3,5-Trinitro-1,3,5-Triazine (RDX) Degradation{triangledown} ,{dagger}

Peter F. Andeer,1 David A. Stahl,1,2 Neil C. Bruce,3 and Stuart E. Strand1,4*

Department of Civil and Environmental Engineering, University of Washington, 201 More Hall, Seattle, Washington 98195-2700,1 Department of Microbiology, University of Washington, Seattle, Washington 98195-7242,2 Centre for Novel Agricultural Products, Department of Biology, University of York, York YO10 5YW, United Kingdom,3 College of Forest Resources, University of Washington, Seattle, Washington 98195-21004

Received 17 October 2008/ Accepted 28 February 2009

Recent studies demonstrated that degradation of the military explosive hexahydro-1,3,5-trinitro-1,3,5-triazine (RDX) by species of Rhodococcus, Gordonia, and Williamsia is mediated by a novel cytochrome P450 with a fused flavodoxin reductase domain (XplA) in conjunction with a flavodoxin reductase (XplB). Pulse field gel analysis was used to localize xplA to extrachromosomal elements in a Rhodococcus sp. and distantly related Microbacterium sp. strain MA1. Comparison of Rhodococcus rhodochrous 11Y and Microbacterium plasmid sequences in the vicinity of xplB and xplA showed near identity (6,710 of 6,721 bp). Sequencing of the associated 52.2-kb region of the Microbacterium plasmid pMA1 revealed flanking insertion sequence elements and additional genes implicated in RDX uptake and degradation.


* Corresponding author. Mailing address: Department of Civil and Environmental Engineering, University of Washington, 201 More Hall, Seattle, WA 98195-2700. Phone: (206) 543-5350. Fax: (206) 685-9185. E-mail: sstrand{at}u.washington.edu

{triangledown} Published ahead of print on 6 March 2009.

{dagger} Supplemental material for this article may be found at http://aem.asm.org/.


Applied and Environmental Microbiology, May 2009, p. 3258-3262, Vol. 75, No. 10
0099-2240/09/$08.00+0     doi:10.1128/AEM.02396-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Sabbadin, F., Jackson, R., Haider, K., Tampi, G., Turkenburg, J. P., Hart, S., Bruce, N. C., Grogan, G. (2009). The 1.5-A Structure of XplA-heme, an Unusual Cytochrome P450 Heme Domain That Catalyzes Reductive Biotransformation of Royal Demolition Explosive. J. Biol. Chem. 284: 28467-28475 [Abstract] [Full Text]