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 Burghout, P.
Right arrow Articles by Koster, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Burghout, P.
Right arrow Articles by Koster, M.

 Previous Article  |  Next Article 

Journal of Bacteriology, July 2004, p. 4645-4654, Vol. 186, No. 14
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.14.4645-4654.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Structure and Electrophysiological Properties of the YscC Secretin from the Type III Secretion System of Yersinia enterocolitica

Peter Burghout,1 Ria van Boxtel,1 Patrick Van Gelder,2 Philippe Ringler,3 Shirley A. Müller,3 Jan Tommassen,1* and Margot Koster1

Department of Molecular Microbiology and Institute of Biomembranes, Utrecht University, 3584 CH Utrecht, The Netherlands,1 Department of Ultrastructure, Flemish Interuniversity Institute of Biotechnology, Free University Brussels, 1050 Brussels, Belgium,2 Maurice E. Müller Institute, Biozentrum, University of Basel, CH-4056 Basel, Switzerland3

Received 23 December 2003/ Accepted 5 April 2004

YscC is the integral outer membrane component of the type III protein secretion machinery of Yersinia enterocolitica and belongs to the family of secretins. This group of proteins forms stable ring-like oligomers in the outer membrane, which are thought to function as transport channels for macromolecules. The YscC oligomer was purified after solubilization from the membrane with a nonionic detergent. Sodium dodecyl sulfate did not dissociate the oligomer, but it caused a change in electrophoretic mobility and an increase in protease susceptibility, indicating partial denaturation of the subunits within the oligomer. The mass of the homo-oligomer, as determined by scanning transmission electron microscopy, was approximately 1 MDa. Analysis of the angular power spectrum from averaged top views of negatively stained YscC oligomers revealed a 13-fold angular order, suggesting that the oligomer consists of 13 subunits. Reconstituted in planar lipid bilayers, the YscC oligomer displayed a constant voltage-independent conductance of approximately 3 nS, thus forming a stable pore. However, in vivo, the expression of YscC did not lead to an increased permeability of the outer membrane. Electron microscopy revealed that the YscC oligomer is composed of three domains, two stacked rings attached to a conical domain. This structure is consistent with the notion that the secretin forms the upper part of the basal body of the needle structure of the type III secreton.

* Corresponding author. Mailing address: Department of Molecular Microbiology, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands. Phone: (31) 30 2532999. Fax: (31) 30 2513655. E-mail: J.P.M.Tommassen{at}bio.uu.nl.

Journal of Bacteriology, July 2004, p. 4645-4654, Vol. 186, No. 14
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.14.4645-4654.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Duret, G., Szymanski, M., Choi, K.-J., Yeo, H.-J., Delcour, A. H. (2008). The TpsB Translocator HMW1B of Haemophilus influenzae Forms a Large Conductance Channel. J. Biol. Chem. 283: 15771-15778 [Abstract] [Full Text]  
  • Zenk, S. F., Stabat, D., Hodgkinson, J. L., Veenendaal, A. K. J., Johnson, S., Blocker, A. J. (2007). Identification of minor inner-membrane components of the Shigella type III secretion system 'needle complex'. Microbiology 153: 2405-2415 [Abstract] [Full Text]  
  • Ogino, T., Ohno, R., Sekiya, K., Kuwae, A., Matsuzawa, T., Nonaka, T., Fukuda, H., Imajoh-Ohmi, S., Abe, A. (2006). Assembly of the Type III Secretion Apparatus of Enteropathogenic Escherichia coli.. J. Bacteriol. 188: 2801-2811 [Abstract] [Full Text]  
  • Chami, M., Guilvout, I., Gregorini, M., Remigy, H. W., Muller, S. A., Valerio, M., Engel, A., Pugsley, A. P., Bayan, N. (2005). Structural Insights into the Secretin PulD and Its Trypsin-resistant Core. J. Biol. Chem. 280: 37732-37741 [Abstract] [Full Text]  
  • Kostakioti, M., Newman, C. L., Thanassi, D. G., Stathopoulos, C. (2005). Mechanisms of Protein Export across the Bacterial Outer Membrane. J. Bacteriol. 187: 4306-4314 [Full Text]  
  • Ghosh, P. (2004). Process of Protein Transport by the Type III Secretion System. Microbiol. Mol. Biol. Rev. 68: 771-795 [Abstract] [Full Text]  
  • Burghout, P., Beckers, F., de Wit, E., van Boxtel, R., Cornelis, G. R., Tommassen, J., Koster, M. (2004). Role of the Pilot Protein YscW in the Biogenesis of the YscC Secretin in Yersinia enterocolitica. J. Bacteriol. 186: 5366-5375 [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»