4.5 Article

Site-directed mutagenesis of the Pseudomonas aeruginosa type III secretion system protein PscJ reveals an essential role for surface-localized residues in needle complex function

期刊

MICROBIAL PATHOGENESIS
卷 45, 期 3, 页码 225-230

出版社

ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.micpath.2008.05.002

关键词

Pseudomonas aeruginosa; Type III secretion; Needle complex; PscJ

资金

  1. NIH [5 R25 GM069516]
  2. Oklahoma Center for the Advancement of Science and Technology [HR03-122]

向作者/读者索取更多资源

The Pseudomonas aeruginosa type III secretion system (TTSS) protein PscJ belongs to the PrgK family of TTSS proteins. These proteins are predicted to form one of the inner membrane localized ring substructures of the TTSS needle complex. To determine which amino acid residues of PscJ are important for its function, the pscJ gene was subjected to site-directed mutagenesis. Fifteen individual PscJ amino acid residues that are located in conserved regions of the PrgK family were targeted for mutagenesis. Eight of these residues could be subjected to non-conservative substitution mutagenesis without affecting the function of the resultant mutant protein. Substitution of the other 7 residues (E26, K52, E105, A107, G126, H133, and V189) resulted in either a non-functional protein or the loss of detectable protein. When the essential residues were mapped on to the crystal structure of the E. coli PrgK homolog EscJ, the majority appeared to localize to surface-exposed regions of the protein suggesting a role for these regions in the assembly of the PscJ ring structure. (C) 2008 Elsevier Ltd. All rights reserved.

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