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 Knight, S. W.
Right arrow Articles by Samuels, D. S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Knight, S. W.
Right arrow Articles by Samuels, D. S.

 Previous Article  |  Next Article 

Journal of Bacteriology, April 2000, p. 2048-2051, Vol. 182, No. 7
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Disruption of the Borrelia burgdorferi gac Gene, Encoding the Naturally Synthesized GyrA C-Terminal Domain

Scott W. Knight,dagger Betsy J. Kimmel, Christian H. Eggers, and D. Scott Samuels*

Division of Biological Sciences, The University of Montana, Missoula, Montana 59812

Received 25 October 1999/Accepted 5 January 2000

The C-terminal domain of the A subunit of DNA gyrase, which we term Gac, is naturally synthesized in Borrelia burgdorferi as an abundant DNA-binding protein. Full-length GyrA, which includes the C-terminal domain, is also synthesized by the spirochete and functions as a subunit of DNA gyrase. We have disrupted synthesis of Gac as an independent protein and demonstrated that it is not essential for growth in a coumarin-resistant background. We detected no alterations in DNA maintenance, condensation, or topology in B. burgdorferi lacking this small DNA-binding protein.

* Corresponding author. Mailing address: Division of Biological Sciences, The University of Montana, 32 Campus Dr. #4824, Missoula MT 59812-4824. Phone: (406) 243-6145. Fax: (406) 243-4184. E-mail: samuels{at}selway.umt.edu.

dagger Present address: Department of Biochemistry/Howard Hughes Medical Institute, 50 North Medical Dr., Salt Lake City, UT 84132.

Journal of Bacteriology, April 2000, p. 2048-2051, Vol. 182, No. 7
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Medrano, M. S., Policastro, P. F., Schwan, T. G., Coburn, J. (2009). Interaction of Borrelia burgdorferi Hbb with the p66 promoter. Nucleic Acids Res 0: gkp1027v1-gkp1027 [Abstract] [Full Text]  
  • Ruthenburg, A. J., Graybosch, D. M., Huetsch, J. C., Verdine, G. L. (2005). A Superhelical Spiral in the Escherichia coli DNA Gyrase A C-terminal Domain Imparts Unidirectional Supercoiling Bias. J. Biol. Chem. 280: 26177-26184 [Abstract] [Full Text]  
  • Corbett, K. D., Shultzaberger, R. K., Berger, J. M. (2004). The C-terminal domain of DNA gyrase A adopts a DNA-bending {beta}-pinwheel fold. Proc. Natl. Acad. Sci. USA 101: 7293-7298 [Abstract] [Full Text]  
  • Frank, K. L., Bundle, S. F., Kresge, M. E., Eggers, C. H., Samuels, D. S. (2003). aadA Confers Streptomycin Resistance in Borrelia burgdorferi. J. Bacteriol. 185: 6723-6727 [Abstract] [Full Text]  
  • Elias, A. F., Stewart, P. E., Grimm, D., Caimano, M. J., Eggers, C. H., Tilly, K., Bono, J. L., Akins, D. R., Radolf, J. D., Schwan, T. G., Rosa, P. (2002). Clonal Polymorphism of Borrelia burgdorferi Strain B31 MI: Implications for Mutagenesis in an Infectious Strain Background. Infect. Immun. 70: 2139-2150 [Abstract] [Full Text]  
  • Hefty, P. S., Jolliff, S. E., Caimano, M. J., Wikel, S. K., Radolf, J. D., Akins, D. R. (2001). Regulation of OspE-Related, OspF-Related, and Elp Lipoproteins of Borrelia burgdorferi Strain 297 by Mammalian Host-Specific Signals. Infect. Immun. 69: 3618-3627 [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»