The XcpR protein of Pseudomonas aeruginosa dimerizes via its N-terminus

Molecular Microbiology
L R TurnerS Lory

Abstract

Extracellular protein secretion by the main terminal branch of the general secretory pathway in Pseudomonas aeruginosa requires a secretion machinery comprising the products of at least 12 genes. One of the components of this machinery, the XcpR protein, belongs to a large family of related proteins distinguished by the presence of a highly conserved nucleotide binding domain (Walker box A). The XcpR protein is essential for the process of extracellular secretion and amino acid substitutions within the Walker A sequence result in inactive XcpR. The same mutations exert a dominant negative effect on protein secretion when expressed in wild-type bacteria. Transdominance of XcpR mutants suggests that this protein is involved in interactions with other components of the secretion machinery or that it functions as a multimer. In this study, the amino-terminal portion of the cl repressor protein of phage lambda was used as a reporter of dimerization in Escherichia coli following fusion to full-length as well as a truncated form of XcpR. The cl-XcpR hybrid proteins were able to dimerize, as demonstrated by the immunity of bacteria expressing them to killing by lambda phage. The full-length XcpR as well as several deletion mutants of X...Continue Reading

Citations

Oct 15, 2003·Journal of Molecular Biology·Mark A RobienWim G J Hol
Mar 21, 2000·Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences·A DanchinP Nitschké
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