Disease relevance of bfpP

• The DNA sequence of this fragment revealed an open reading frame, designated bfpP, the predicted product of which is homologous to other prepilin peptidases, including TcpJ of Vibrio cholerae (30% identical amino acids), PulO of Klebsiella oxytoca (29%), and PilD of P. aeruginosa (28%) [1].
• A plasmid-encoded prepilin peptidase gene from enteropathogenic Escherichia coli [1].
• Protein secretion in Pseudomonas aeruginosa: characterization of seven xcp genes and processing of secretory apparatus components by prepilin peptidase [2].
• Identification of the Vibrio cholerae type 4 prepilin peptidase required for cholera toxin secretion and pilus formation [3].
• Escherichia coli K-12 strains grown at 37 degrees C or 42 degrees C, but not at 30 degrees C, process the precursors of the Neisseria gonorrhoeae type IV pilin PilE and the Klebsiella oxytoca type IV pseudopilin PulG in a manner reminiscent of the prepilin peptidase-dependent processing of these proteins that occurs in these bacteria [4].

High impact information on bfpP

• Processing of prePulG in Escherichia coli requires a glycine at position -1, as does processing by the cognate prepilin peptidase (PulO), and is unaffected by mutations that inactivate several non-specific proteases [4].
• PppA was able to replace PulO prepilin peptidase in a pullulanase secretion system reconstituted in E. coli when expressed from high-copy-number plasmids but not when present in a single chromosomal copy [4].
• This prepilin peptidase cleavage site is present in the products of four genes in the pulC-O operon (PulG, PulH, Pull and PulJ proteins) [5].
• The mutation in bfpP, the prepilin peptidase gene, does not affect prebundlin expression but blocks signal sequence cleavage of prebundlin, BFP biogenesis, and LA [6].
• One of them, a pilin-like protein, EpsG, was analyzed also in V. cholerae and found to migrate as two bands on polyacrylamide gels, suggesting that in this organism it might be processed or otherwise modified by a prepilin peptidase [7].

Biological context of bfpP

• We cloned restriction fragments downstream of the bfpA gene into an E. coli-Pseudomonas aeruginosa shuttle vector and mobilized them into a P. aeruginosa prepilin peptidase (pilD) mutant [1].
• A plasmid-encoded gene cluster encodes bundlin, the major structural subunit of a type-IV fimbria called the bundle-forming pilus (BFP), a prepilin peptidase necessary for processing of pre-bundlin to its mature form, and twelve other proteins [8].

Other interactions of bfpP

• When complemented with a larger fragment containing bfpP as well as bfpA, the mutant expresses the fully processed BfpA protein [1].

Analytical, diagnostic and therapeutic context of bfpP

• We have used a PCR amplification strategy to clone the N. gonorrhoeae prepilin peptidase gene, pilDNg [9].
• Western blot analysis of CofA reveals that CofA is produced initially as a 26.5-kDa preform pilin (prepilin) and then processed to 20.5-kDa mature pilin by a prepilin peptidase [10].

References