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 Hamad, M. A.
Right arrow Articles by Nilles, M. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hamad, M. A.
Right arrow Articles by Nilles, M. L.

 Previous Article  |  Next Article 

Journal of Bacteriology, September 2007, p. 6734-6739, Vol. 189, No. 18
0021-9193/07/$08.00+0     doi:10.1128/JB.00539-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Structure-Function Analysis of the C-Terminal Domain of LcrV from Yersinia pestis{triangledown}

Mohamad A. Hamad{dagger} and Matthew L. Nilles*

Department of Microbiology and Immunology, University of North Dakota School of Medicine and Health Sciences, Grand Forks, North Dakota 58202

Received 9 April 2007/ Accepted 18 June 2007

LcrV, a multifunctional protein, acts as a positive regulator of effector protein secretion for the type III secretion system (T3SS) in Yersinia pestis by interaction with the negative regulator LcrG. In this study, LcrV was analyzed to identify regions required for LcrG interaction. Random-linker insertion mutagenesis, deletion analysis, and site-directed mutagenesis of hydrophobic amino acids between residues 290 and 311 allowed the isolation of an LcrV mutant (LcrV L291R F308R) defective for LcrG interaction. The new residues identified in LcrG interaction lie in helix 12 of LcrV; residues in helix 7 of LcrV are known to be involved in LcrG interaction. Helix 7 and helix 12 of LcrV interact to form an intramolecular coiled coil; these new results suggest that the intramolecular coiled coil in LcrV is required for LcrG interaction and activation of the T3SS.

* Corresponding author. Mailing address: University of North Dakota, Dept. of Microbiol. and Immunol. Room 4700, School of Medicine and Health Sciences, 501 N. Columbia Road, Stop 9037, Grand Forks, ND 58203-9037. Phone: (701) 777-2750. Fax: (701) 777-2054. E-mail: mnilles{at}medicine.nodak.edu

{triangledown} Published ahead of print on 20 July 2007.

{dagger} Present address: University of Colorado, Health Sciences Center, MS#8333, Department of Microbiology, RC-1 North, East 19th Ave, Room 9402A, Aurora, CO 80045-6511.

Journal of Bacteriology, September 2007, p. 6734-6739, Vol. 189, No. 18
0021-9193/07/$08.00+0     doi:10.1128/JB.00539-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Caroline, G., Eric, F., Bohn, Y.-S. T., Sylvie, E., Attree, I. (2008). Oligomerization of PcrV and LcrV, Protective Antigens of Pseudomonas aeruginosa and Yersinia pestis. J. Biol. Chem. 283: 23940-23949 [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»