http://purl.uniprot.org/citations/23255525 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/23255525 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/23255525 | http://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/23255525 | http://purl.org/dc/terms/identifier | "doi:10.1002/mbo3.51"xsd:string |
http://purl.uniprot.org/citations/23255525 | http://purl.org/dc/terms/identifier | "doi:10.1002/mbo3.51"xsd:string |
http://purl.uniprot.org/citations/23255525 | http://purl.uniprot.org/core/author | "Makino S."xsd:string |
http://purl.uniprot.org/citations/23255525 | http://purl.uniprot.org/core/author | "Makino S."xsd:string |
http://purl.uniprot.org/citations/23255525 | http://purl.uniprot.org/core/author | "Fox B.G."xsd:string |
http://purl.uniprot.org/citations/23255525 | http://purl.uniprot.org/core/author | "Fox B.G."xsd:string |
http://purl.uniprot.org/citations/23255525 | http://purl.uniprot.org/core/author | "Goren M.A."xsd:string |
http://purl.uniprot.org/citations/23255525 | http://purl.uniprot.org/core/author | "Goren M.A."xsd:string |
http://purl.uniprot.org/citations/23255525 | http://purl.uniprot.org/core/author | "Chan C.H."xsd:string |
http://purl.uniprot.org/citations/23255525 | http://purl.uniprot.org/core/author | "Chan C.H."xsd:string |
http://purl.uniprot.org/citations/23255525 | http://purl.uniprot.org/core/author | "Beebe E.T."xsd:string |
http://purl.uniprot.org/citations/23255525 | http://purl.uniprot.org/core/author | "Beebe E.T."xsd:string |
http://purl.uniprot.org/citations/23255525 | http://purl.uniprot.org/core/author | "Forest K.T."xsd:string |
http://purl.uniprot.org/citations/23255525 | http://purl.uniprot.org/core/author | "Forest K.T."xsd:string |
http://purl.uniprot.org/citations/23255525 | http://purl.uniprot.org/core/author | "Aly K.A."xsd:string |
http://purl.uniprot.org/citations/23255525 | http://purl.uniprot.org/core/author | "Aly K.A."xsd:string |
http://purl.uniprot.org/citations/23255525 | http://purl.uniprot.org/core/author | "Sepulveda C."xsd:string |
http://purl.uniprot.org/citations/23255525 | http://purl.uniprot.org/core/author | "Sepulveda C."xsd:string |
http://purl.uniprot.org/citations/23255525 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
http://purl.uniprot.org/citations/23255525 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
http://purl.uniprot.org/citations/23255525 | http://purl.uniprot.org/core/name | "MicrobiologyOpen"xsd:string |
http://purl.uniprot.org/citations/23255525 | http://purl.uniprot.org/core/name | "MicrobiologyOpen"xsd:string |