| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
|
|
|
|||||||
|
|||||||||
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Papers In Press, published online ahead of print March 29, 2005
DOE Plant Research Laboratory, Michigan State University, East Lansing, MI 48824
Corresponding Author: hes{at}msu.edu
The Hrp pilus plays an essential role in the long-distance type III translocation of effector proteins from bacteria into plant cells. HrpA is the structural subunit of the Hrp pilus in Pseudomonas syringae pv. tomato (Pst) DC3000. Little is known about the molecular features in the HrpA protein for pilus assembly or for transporting effector proteins. From previous collections of nonfunctional HrpA derivatives that carry random pentapeptide insertions or single amino acid mutations, we identified several dominant-negative mutants that blocked the ability of wild-type Pst DC3000 to elicit host responses. The dominant-negative phenotype was correlated with the disappearance of the Hrp pilus in culture and inhibition of the wild-type HrpA protein to self-assemble in vitro. Dominant-negative HrpA mutants can be grouped into two functional classes, one class exerted a strong dominant-negative effect on the secretion of effector proteins AvrPto and HopPtoM in culture, and the other did not. The two classes of mutant HrpA proteins carry pentapeptide insertions in discrete regions, which are interrupted by insertions without a dominant-negative effect. These results enable prediction of possible subunit-subunit interaction sites in the assembly of the Hrp pilus, and suggest the usefulness of dominant-negative mutants in the dissection of the role of the wild-type HrpA protein in various stages of type III translocation: protein exit across the bacterial cell wall, the assembly and/or stabilization of the Hrp pilus in the extracellular space, and Hrp pilus-mediated long-distance transport beyond the bacterial cell wall.
J. Biol. Chem, 10.1074/jbc.M500972200
Submitted on January 26, 2005
Revised on March 3, 2005
Accepted on March 29, 2005
Use of dominant-negative HrpA mutants to dissect Hrp pilus assembly and type III secretion in Pseudomonas syringae pv. tomato
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  D. S. Guttman, S. J. Gropp, R. L. Morgan, and P. W. Wang Diversifying Selection Drives the Evolution of the Type III Secretion System Pilus of Pseudomonas syringae Mol. Biol. Evol., December 1, 2006; 23(12): 2342 - 2354. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 C.-W. Yang, R. Gonzalez-Lamothe, R. A. Ewan, O. Rowland, H. Yoshioka, M. Shenton, H. Ye, E. O'Donnell, J. D.G. Jones, and A. Sadanandom The E3 Ubiquitin Ligase Activity of Arabidopsis PLANT U-BOX17 and Its Functional Tobacco Homolog ACRE276 Are Required for Cell Death and Defense PLANT CELL, April 1, 2006; 18(4): 1084 - 1098. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 R. Kenjale, J. Wilson, S. F. Zenk, S. Saurya, W. L. Picking, W. D. Picking, and A. Blocker The Needle Component of the Type III Secreton of Shigella Regulates the Activity of the Secretion Apparatus J. Biol. Chem., December 30, 2005; 280(52): 42929 - 42937. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 E. Weber and R. Koebnik Domain Structure of HrpE, the Hrp Pilus Subunit of Xanthomonas campestris pv. vesicatoria J. Bacteriol., September 1, 2005; 187(17): 6175 - 6186. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |
