This Article
Right arrow Full Text
Right arrow Full Text (PDF)
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 Nagata, Y.
Right arrow Articles by Takagi, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Nagata, Y.
Right arrow Articles by Takagi, M.

 Previous Article  |  Next Article 

Journal of Bacteriology, September 1999, p. 5409-5413, Vol. 181, No. 17
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Two Different Types of Dehalogenases, LinA and LinB, Involved in gamma -Hexachlorocyclohexane Degradation in Sphingomonas paucimobilis UT26 Are Localized in the Periplasmic Space without Molecular Processing

Yuji Nagata,* Akiko Futamura, Keisuke Miyauchi, and Masamichi Takagi

Department of Biotechnology, The University of Tokyo, Bunkyo-ku, Tokyo 113-8657, Japan

Received 8 March 1999/Accepted 11 June 1999

gamma -Hexachlorocyclohexane (gamma -HCH) is one of several highly chlorinated insecticides that cause serious environmental problems. The cellular proteins of a gamma -HCH-degrading bacterium, Sphingomonas paucimobilis UT26, were fractionated into periplasmic, cytosolic, and membrane fractions after osmotic shock. Most of two different types of dehalogenase, LinA (gamma -hexachlorocyclohexane dehydrochlorinase) and LinB (1,3,4,6-tetrachloro-1,4-cyclohexadiene halidohydrolase), that are involved in the early steps of gamma -HCH degradation in UT26 was detected in the periplasmic fraction and had not undertaken molecular processing. Furthermore, immunoelectron microscopy clearly showed that LinA and LinB are periplasmic proteins. LinA and LinB both lack a typical signal sequence for export, so they may be secreted into the periplasmic space via a hitherto unknown mechanism.

* Corresponding author. Mailing address: Department of Biotechnology, The University of Tokyo, Yayoi 1-1-1, Bunkyo-ku, Tokyo 113-8657, Japan. Phone: 81-3-5841-5178. Fax: 81-3-5841-8015. E-mail: aynaga{at}hongo.ecc.u-tokyo.ac.jp.

Journal of Bacteriology, September 1999, p. 5409-5413, Vol. 181, No. 17
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Endo, R., Ohtsubo, Y., Tsuda, M., Nagata, Y. (2007). Identification and Characterization of Genes Encoding a Putative ABC-Type Transporter Essential for Utilization of {gamma}-Hexachlorocyclohexane in Sphingobium japonicum UT26. J. Bacteriol. 189: 3712-3720 [Abstract] [Full Text]  
  • Fortin, P. D., Horsman, G. P., Yang, H. M., Eltis, L. D. (2006). A glutathione s-transferase catalyzes the dehalogenation of inhibitory metabolites of polychlorinated biphenyls.. J. Bacteriol. 188: 4424-4430 [Abstract] [Full Text]  
  • Mertens, B., Boon, N., Verstraete, W. (2006). Slow-Release Inoculation Allows Sustained Biodegradation of {gamma}-Hexachlorocyclohexane. Appl. Environ. Microbiol. 72: 622-627 [Abstract] [Full Text]  
  • Nagata, Y., Prokop, Z., Sato, Y., Jerabek, P., Kumar, A., Ohtsubo, Y., Tsuda, M., Damborsky, J. (2005). Degradation of {beta}-Hexachlorocyclohexane by Haloalkane Dehalogenase LinB from Sphingomonas paucimobilis UT26. Appl. Environ. Microbiol. 71: 2183-2185 [Abstract] [Full Text]  
  • Kumari, R., Subudhi, S., Suar, M., Dhingra, G., Raina, V., Dogra, C., Lal, S., van der Meer, J. R., Holliger, C., Lal, R. (2002). Cloning and Characterization of lin Genes Responsible for the Degradation of Hexachlorocyclohexane Isomers by Sphingomonas paucimobilis Strain B90. Appl. Environ. Microbiol. 68: 6021-6028 [Abstract] [Full Text]  
  • Kamath, S., Chen, M. L., Chakrabarty, A. M. (2000). Secretion of Nucleoside Diphosphate Kinase by Mucoid Pseudomonas aeruginosa 8821: Involvement of a Carboxy-Terminal Motif in Secretion. J. Bacteriol. 182: 3826-3831 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»