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 Boyle, D. S.
Right arrow Articles by Donachie, W. D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Boyle, D. S.
Right arrow Articles by Donachie, W. D.

 Previous Article

Journal of Bacteriology, July 2000, p. 4124-4127, Vol. 182, No. 14
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

All Major Regions of FtsK Are Required for Resolution of Chromosome Dimers

David S. Boyle,* Dawn Grant, G. Craig Draper,dagger and William D. Donachie

Institute of Cell & Molecular Biology, University of Edinburgh, Edinburgh EH9 3JR, Scotland

Received 20 December 1999/Accepted 13 April 2000

Resolution of chromosome dimers, by site-specific recombination between dif sites, is carried out in Escherichia coli by XerCD recombinase in association with the FtsK protein. We show here that a variety of altered FtsK polypeptides, consisting of the N-terminal (cell division) domain alone or with deletions in the proline-glutamine-rich part of the protein, or polypeptides consisting of the C-terminal domain alone are all unable to carry out dif recombination. Alteration of the putative nucleotide-binding site also abolishes the ability of FtsK to carry out recombination between dif sites.

* Corresponding author. Present address: Sidney Kimmel Cancer Center, 10835 Altman Row, San Diego, CA 92121. Phone: (858) 450-5990, ext. 257. Fax: (858) 550-3998. E-mail: Dboyle{at}skcc.org.

dagger Present address: Department of Chemistry & Biochemistry, University of California at Los Angeles, Los Angeles, CA 90095.

Journal of Bacteriology, July 2000, p. 4124-4127, Vol. 182, No. 14
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Shi, Q., Huguet-Tapia, J. C., Peters, J. E. (2009). Tn917 Targets the Region Where DNA Replication Terminates in Bacillus subtilis, Highlighting a Difference in Chromosome Processing in the Firmicutes. J. Bacteriol. 191: 7623-7627 [Abstract] [Full Text]  
  • Wang, S. C. E., West, L., Shapiro, L. (2006). The Bifunctional FtsK Protein Mediates Chromosome Partitioning and Cell Division in Caulobacter. J. Bacteriol. 188: 1497-1508 [Abstract] [Full Text]  
  • Dohmann, K., Strommenger, B., Stevenson, K., de Juan, L., Stratmann, J., Kapur, V., Bull, T. J., Gerlach, G.-F. (2003). Characterization of Genetic Differences between Mycobacterium avium subsp. paratuberculosis Type I and Type II Isolates. J. Clin. Microbiol. 41: 5215-5223 [Abstract] [Full Text]  
  • Akerlund, T., Gullbrand, B., Nordstrom, K. (2002). Effects of the Min system on nucleoid segregation in Escherichia coli. Microbiology 148: 3213-3222 [Abstract] [Full Text]  
  • McCool, J. D., Sandler, S. J. (2001). Effects of mutations involving cell division, recombination, and chromosome dimer resolution on a priA2::kan mutant. Proc. Natl. Acad. Sci. USA 98: 8203-8210 [Abstract] [Full Text]  
  • Sciochetti, S. A., Piggot, P. J., Blakely, G. W. (2001). Identification and Characterization of the dif Site from Bacillus subtilis. J. Bacteriol. 183: 1058-1068 [Abstract] [Full Text]  
  • Barre, F.-X., Aroyo, M., Colloms, S. D., Helfrich, A., Cornet, F., Sherratt, D. J. (2000). FtsK functions in the processing of a Holliday junction intermediate during bacterial chromosome segregation. Genes Dev. 14: 2976-2988 [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»