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 Smith, M. C. A.
Right arrow Articles by Thomas, C. D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Smith, M. C. A.
Right arrow Articles by Thomas, C. D.

 Previous Article  |  Next Article 

Journal of Bacteriology, June 2004, p. 3363-3373, Vol. 186, No. 11
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.11.3363-3373.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

An Accessory Protein Is Required for Relaxosome Formation by Small Staphylococcal Plasmids

Matthew C. A. Smith{dagger} and Christopher D. Thomas*

Astbury Centre for Structural Molecular Biology, School of Biochemistry and Molecular Biology, University of Leeds, Leeds LS2 9JT, United Kingdom

Received 4 August 2003/ Accepted 11 February 2004

Mobilization of the staphylococcal plasmid pC221 requires at least one plasmid-encoded protein, MobA, in order to form a relaxosome. pC221 and closely related plasmids also possess an overlapping reading frame encoding a protein of 15 kDa, termed MobC. By completing the nucleotide sequence of plasmid pC223, we have found a further example of this small protein, and gene knockouts have shown that MobC is essential for relaxosome formation and plasmid mobilization in both pC221 and pC223. Primer extension analysis has been used to identify the nic site in both of these plasmids, located upstream of the mobC gene in the sense strand. Although the sequence surrounding the nic site is highly conserved between pC221 and pC223, exchange of the oriT sequence between plasmids significantly reduces the extent of relaxation complex formation, suggesting that the Mob proteins are selective for their cognate plasmids in vivo.

* Corresponding author. Mailing address: Astbury Centre for Structural Molecular Biology, School of Biochemistry and Molecular Biology, University of Leeds, Leeds LS2 9JT, United Kingdom. Phone: 44/0 113-343-3040. Fax: 44/0 113-343-1407. E-mail: cdt{at}bmb.leeds.ac.uk.

{dagger} Present address: Institute of Genetics, University of Nottingham, Queen's Medical Centre, Nottingham NG7 2UH, United Kingdom.

Journal of Bacteriology, June 2004, p. 3363-3373, Vol. 186, No. 11
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.11.3363-3373.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Varsaki, A., Moncalian, G., del Pilar Garcillan-Barcia, M., Drainas, C., de la Cruz, F. (2009). Analysis of ColE1 MbeC Unveils an Extended Ribbon-Helix-Helix Family of Nicking Accessory Proteins. J. Bacteriol. 191: 1446-1455 [Abstract] [Full Text]  
  • Lorenzo-Diaz, F., Espinosa, M. (2009). Lagging-Strand DNA Replication Origins Are Required for Conjugal Transfer of the Promiscuous Plasmid pMV158. J. Bacteriol. 191: 720-727 [Abstract] [Full Text]  
  • Chen, Y., Zhang, X., Manias, D., Yeo, H.-J., Dunny, G. M., Christie, P. J. (2008). Enterococcus faecalis PcfC, a Spatially Localized Substrate Receptor for Type IV Secretion of the pCF10 Transfer Intermediate. J. Bacteriol. 190: 3632-3645 [Abstract] [Full Text]  
  • Arraiano, C. M., Bamford, J., Brussow, H., Carpousis, A. J., Pelicic, V., Pfluger, K., Polard, P., Vogel, J. (2007). Recent Advances in the Expression, Evolution, and Dynamics of Prokaryotic Genomes. J. Bacteriol. 189: 6093-6100 [Full Text]  
  • Criado, R., Diep, D. B., Aakra, A., Gutierrez, J., Nes, I. F., Hernandez, P. E., Cintas, L. M. (2006). Complete Sequence of the Enterocin Q-Encoding Plasmid pCIZ2 from the Multiple Bacteriocin Producer Enterococcus faecium L50 and Genetic Characterization of Enterocin Q Production and Immunity.. Appl. Environ. Microbiol. 72: 6653-6666 [Abstract] [Full Text]  
  • Caryl, J. A., Smith, M. C. A., Thomas, C. D. (2004). Reconstitution of a Staphylococcal Plasmid-Protein Relaxation Complex In Vitro. J. Bacteriol. 186: 3374-3383 [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»