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http://purl.uniprot.org/citations/23255525http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23255525http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23255525http://www.w3.org/2000/01/rdf-schema#comment"Integral membrane aspartic acid proteases are receiving growing recognition for their fundamental roles in cellular physiology of eukaryotes and prokaryotes, and may be medically important pharmaceutical targets. The Gram-negative Pseudomonas aeruginosa PilD and the archaeal Methanococcus voltae FlaK were synthesized in the presence of unilamellar liposomes in a cell-free translation system. Cosynthesis of PilD with its full-length substrate, PilA, or of FlaK with its full-length substrate, FlaB2, led to complete cleavage of the substrate signal peptides. Scaled-up synthesis of PilD, followed by solubilization in dodecyl-β-d-maltoside and chromatography, led to a pure enzyme that retained both of its known biochemical activities: cleavage of the PilA signal peptide and S-adenosyl methionine-dependent methylation of the mature pilin. X-ray fluorescence scans show for the first time that PilD is a zinc-binding protein. Zinc is required for the N-terminal methylation of the mature pilin, but not for signal peptide cleavage. Taken together, our work identifies the P. aeruginosa prepilin peptidase PilD as a zinc-dependent N-methyltransferase and provides a new platform for large-scale synthesis of PilD and other integral membrane proteases important for basic microbial physiology and virulence."xsd:string
http://purl.uniprot.org/citations/23255525http://purl.org/dc/terms/identifier"doi:10.1002/mbo3.51"xsd:string
http://purl.uniprot.org/citations/23255525http://purl.org/dc/terms/identifier"doi:10.1002/mbo3.51"xsd:string
http://purl.uniprot.org/citations/23255525http://purl.uniprot.org/core/author"Makino S."xsd:string
http://purl.uniprot.org/citations/23255525http://purl.uniprot.org/core/author"Makino S."xsd:string
http://purl.uniprot.org/citations/23255525http://purl.uniprot.org/core/author"Fox B.G."xsd:string
http://purl.uniprot.org/citations/23255525http://purl.uniprot.org/core/author"Fox B.G."xsd:string
http://purl.uniprot.org/citations/23255525http://purl.uniprot.org/core/author"Goren M.A."xsd:string
http://purl.uniprot.org/citations/23255525http://purl.uniprot.org/core/author"Goren M.A."xsd:string
http://purl.uniprot.org/citations/23255525http://purl.uniprot.org/core/author"Chan C.H."xsd:string
http://purl.uniprot.org/citations/23255525http://purl.uniprot.org/core/author"Chan C.H."xsd:string
http://purl.uniprot.org/citations/23255525http://purl.uniprot.org/core/author"Beebe E.T."xsd:string
http://purl.uniprot.org/citations/23255525http://purl.uniprot.org/core/author"Beebe E.T."xsd:string
http://purl.uniprot.org/citations/23255525http://purl.uniprot.org/core/author"Forest K.T."xsd:string
http://purl.uniprot.org/citations/23255525http://purl.uniprot.org/core/author"Forest K.T."xsd:string
http://purl.uniprot.org/citations/23255525http://purl.uniprot.org/core/author"Aly K.A."xsd:string
http://purl.uniprot.org/citations/23255525http://purl.uniprot.org/core/author"Aly K.A."xsd:string
http://purl.uniprot.org/citations/23255525http://purl.uniprot.org/core/author"Sepulveda C."xsd:string
http://purl.uniprot.org/citations/23255525http://purl.uniprot.org/core/author"Sepulveda C."xsd:string
http://purl.uniprot.org/citations/23255525http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23255525http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23255525http://purl.uniprot.org/core/name"MicrobiologyOpen"xsd:string
http://purl.uniprot.org/citations/23255525http://purl.uniprot.org/core/name"MicrobiologyOpen"xsd:string