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Journal of Bacteriology, November 2006, p. 7378-7386, Vol. 188, No. 21
0021-9193/06/$08.00+0     doi:10.1128/JB.00760-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Differential Telomere Processing by Borrelia Telomere Resolvases In Vitro but Not In Vivo{triangledown}

Yvonne Tourand,1,2 Troy Bankhead,1 Sandra L. Wilson,1 Adrienne D. Putteet-Driver,3 Alan G. Barbour,3 Rebecca Byram,4 Patricia A. Rosa,4 and George Chaconas1*

Department of Biochemistry and Molecular Biology and Department of Microbiology and Infectious Diseases, University of Calgary, Calgary, Alberta T2N 4N1, Canada,1 Department of Microbiology and Immunology, University of Western Ontario, London, Ontario N6A 5C1, Canada,2 Departments of Microbiology and Molecular Genetics and Medicine, University of California Irvine, Irvine, California 92697-4025,3 Laboratory of Zoonotic Pathogens, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, Montana 598404

Received 26 May 2006/ Accepted 14 August 2006

Causative agents of Lyme disease and relapsing fever, including Borrelia burgdorferi and Borrelia hermsii, respectively, are unusual among bacteria in that they possess a segmented genome with linear DNA molecules terminated by hairpin ends, known as telomeres. During replication, these telomeres are processed by the essential telomere resolvase, ResT, in a unique biochemical reaction known as telomere resolution. In this study, we report the identification of the B. hermsii resT gene through cross-species hybridization. Sequence comparison of the B. hermsii protein with the B. burgdorferi orthologue revealed 67% identity, including all the regions currently known to be crucial for telomere resolution. In vitro studies, however, indicated that B. hermsii ResT was unable to process a replicated B. burgdorferi type 2 telomere substrate. In contrast, in vivo cross-species complementation in which the native resT gene of B. burgdorferi was replaced with B. hermsii resT had no discernible effect, even though B. burgdorferi strain B31 carries at least two type 2 telomere ends. The B. burgdorferi ResT protein was also able to process two telomere spacing mutants in vivo that were unresolvable in vitro. The unexpected differential telomere processing in vivo versus in vitro by the two telomere resolvases suggests the presence of one or more accessory factors in vivo that are normally involved in the reaction. Our current results are also expected to facilitate further studies into ResT structure and function, including possible interaction with other Borrelia proteins.

* Corresponding author. Mailing address: Department of Biochemistry and Molecular Biology, University of Calgary, Calgary, Alberta T2N 4N1 Canada. Phone: (403) 210-9692. Fax: (403) 270-2772. E-mail: chaconas{at}ucalgary.ca.

{triangledown} Published ahead of print on 25 August 2006.

Journal of Bacteriology, November 2006, p. 7378-7386, Vol. 188, No. 21
0021-9193/06/$08.00+0     doi:10.1128/JB.00760-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Tourand, Y., Deneke, J., Moriarty, T. J., Chaconas, G. (2009). Characterization and in Vitro Reaction Properties of 19 Unique Hairpin Telomeres from the Linear Plasmids of the Lyme Disease Spirochete. J. Biol. Chem. 284: 7264-7272 [Abstract] [Full Text]  
  • Welsh, E. A., Liberton, M., Stockel, J., Loh, T., Elvitigala, T., Wang, C., Wollam, A., Fulton, R. S., Clifton, S. W., Jacobs, J. M., Aurora, R., Ghosh, B. K., Sherman, L. A., Smith, R. D., Wilson, R. K., Pakrasi, H. B. (2008). The genome of Cyanothece 51142, a unicellular diazotrophic cyanobacterium important in the marine nitrogen cycle. Proc. Natl. Acad. Sci. USA 105: 15094-15099 [Abstract] [Full Text]  
  • Deneke, J., Chaconas, G. (2008). Purification and Properties of the Plasmid Maintenance Proteins from the Borrelia burgdorferi Linear Plasmid lp17. J. Bacteriol. 190: 3992-4000 [Abstract] [Full Text]  


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