This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental material
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 Google Scholar
Google Scholar
Right arrow Articles by Steen, J. A.
Right arrow Articles by Rood, J. I.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Steen, J. A.
Right arrow Articles by Rood, J. I.

 Previous Article  |  Next Article 

Journal of Bacteriology, May 2009, p. 2926-2933, Vol. 191, No. 9
0021-9193/09/$08.00+0     doi:10.1128/JB.00032-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

The Putative Coupling Protein TcpA Interacts with Other pCW3-Encoded Proteins To Form an Essential Part of the Conjugation Complex{triangledown} ,{dagger}

Jennifer A. Steen,1 Trudi L. Bannam,1 Wee Lin Teng,1 Rodney J. Devenish,2 and Julian I. Rood1*

Australian Research Council Centre of Excellence in Structural and Functional Microbial Genomics, Departments of Microbiology,1 Biochemistry Molecular Biology, Monash University, Clayton, Victoria 3800, Australia2

Received 12 January 2009/ Accepted 18 February 2009

Conjugative plasmids encode antibiotic resistance determinants or toxin genes in the anaerobic pathogen Clostridium perfringens. The paradigm conjugative plasmid in this bacterium is pCW3, a 47-kb tetracycline resistance plasmid that encodes the unique tcp transfer locus. The tcp locus consists of 11 genes, intP and tcpA-tcpJ, at least three of which, tcpA, tcpF, and tcpH, are essential for the conjugative transfer of pCW3. In this study we examined protein-protein interactions involving TcpA, the putative coupling protein. Use of a bacterial two-hybrid system identified interactions between TcpA and TcpC, TcpG, and TcpH. This analysis also demonstrated TcpA, TcpC, and TcpG self-interactions, which were confirmed by chemical cross-linking studies. Examination of a series of deletion and site-directed derivatives of TcpA identified the domains and motifs required for these interactions. Based on these results, we have constructed a model for this unique conjugative transfer apparatus.


* Corresponding author. Mailing address: Department of Microbiology, Monash University, Clayton, Victoria 3800, Australia. Phone: 61 3 9902 9157. Fax: 61 3 9902 9222. E-mail: julian.rood{at}med.monash.edu.au

{triangledown} Published ahead of print on 27 February 2009.

{dagger} Supplemental material for this article may be found at http://jb.asm.org/.


Journal of Bacteriology, May 2009, p. 2926-2933, Vol. 191, No. 9
0021-9193/09/$08.00+0     doi:10.1128/JB.00032-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.