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 Van Arnam, J. S.
Right arrow Articles by Macnab, R. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Van Arnam, J. S.
Right arrow Articles by Macnab, R. M.

 Previous Article  |  Next Article 

Journal of Bacteriology, April 2004, p. 2495-2498, Vol. 186, No. 8
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.8.2495-2498.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Analysis of an Engineered Salmonella Flagellar Fusion Protein, FliR-FlhB{dagger}

John S. Van Arnam, Jonathan L. McMurry, May Kihara,* and Robert M. Macnab

Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520

Received 17 November 2003/ Accepted 9 January 2004

Salmonella FliR and FlhB are membrane proteins necessary for flagellar export. In Clostridium a fliR-flhB fusion gene exists. We constructed a similar Salmonella fusion gene which is able to complement fliR, flhB, and fliR flhB null strains. Western blotting revealed that the FliR-FlhB fusion protein retains the FlhB protein's cleavage properties. We conclude that the FliR and FlhB proteins are physically associated in the wild-type Salmonella basal body, probably in a 1:1 ratio.

* Corresponding author. Mailing address: Yale University, Department of Molecular Biophysics and Biochemistry 0734, 266 Whitney Ave., P.O. Box 208114, New Haven, CT 06520-8114. Phone: (203) 432-5588. Fax: (203) 432-9782. E-mail: may.macnab{at}yale.edu.

{dagger} This paper is dedicated to Robert Macnab, who died suddenly on 7 September 2003.

Journal of Bacteriology, April 2004, p. 2495-2498, Vol. 186, No. 8
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.8.2495-2498.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Rust, M., Borchert, S., Niehus, E., Kuehne, S. A., Gripp, E., Bajceta, A., McMurry, J. L., Suerbaum, S., Hughes, K. T., Josenhans, C. (2009). The Helicobacter pylori Anti-Sigma Factor FlgM Is Predominantly Cytoplasmic and Cooperates with the Flagellar Basal Body Protein FlhA. J. Bacteriol. 191: 4824-4834 [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]  
  • Wand, M. E., Sockett, R. E., Evans, K. J., Doherty, N., Sharp, P. M., Hardie, K. R., Winzer, K. (2006). Helicobacter pylori FlhB Function: the FlhB C-Terminal Homologue HP1575 Acts as a "Spare Part" To Permit Flagellar Export When the HP0770 FlhBCC Domain Is Deleted.. J. Bacteriol. 188: 7531-7541 [Abstract] [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]  
  • McMurry, J. L., Van Arnam, J. S., Kihara, M., Macnab, R. M. (2004). Analysis of the Cytoplasmic Domains of Salmonella FlhA and Interactions with Components of the Flagellar Export Machinery. J. Bacteriol. 186: 7586-7592 [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»