| http://purl.uniprot.org/citations/3141383 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/3141383 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/3141383 | http://www.w3.org/2000/01/rdf-schema#comment | "Three cell-associated elastase precursors with approximate molecular weights of 60,000 (P), 56,000 (Pro I), and 36,000 (Pro II) were identified in Pseudomonas aeruginosa cells by pulse-labeling with [35S]methionine and immunoprecipitation. In the absence of inhibitors, cells of a wild-type strain as well as those of the secretion-defective mutant PAKS 18 accumulated Pro II as the only elastase-related radioactive protein. EDTA but not EGTA [ethylene glycol-bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid] inhibited the formation of Pro II, and this inhibition was accompanied by the accumulation of Pro I. P accumulated in cells labeled in the presence of ethanol (with or without EDTA), dinitrophenol plus EDTA, or carbonyl cyanide m-chlorophenyl hydrazone plus EDTA. Pro I and Pro II were localized to the periplasm, and as evident from pulse-chase experiments, Pro I was converted to the mature extracellular enzyme with Pro II as an intermediate of the reaction. P was located to the membrane fraction. Pro I but not Pro II was immunoprecipitated by antibodies specific to a protein of about 20,000 molecular weight (P20), which, as we showed before (Kessler and Safrin, J. Bacteriol. 170:1215-1219, 1988), forms a complex with an inactive periplasmic elastase precursor of about 36,000 molecular weight. Our results suggest that the elastase is made by the cells as a preproenzyme (P), containing a signal sequence of about 4,000 molecular weight and a "pro" sequence of about 20,000 molecular weight. Processing and export of the preproenzyme involve the formation of two periplasmic proenzyme species: proelastase I (56 kilodaltons [kDa]) and proelastase II (36 kDa). The former is short-lived, whereas proelastase II accumulates temporarily in the periplasm, most likely as a complex with the 20-kDa propeptide released from proelastase I upon conversion to proelastase II. The final step in elastase secretion seems to required both the proteolytic removal of a small peptide from proelastase II and dissociation of the latter from P20."xsd:string |
| http://purl.uniprot.org/citations/3141383 | http://purl.org/dc/terms/identifier | "doi:10.1128/jb.170.11.5241-5247.1988"xsd:string |
| http://purl.uniprot.org/citations/3141383 | http://purl.org/dc/terms/identifier | "doi:10.1128/jb.170.11.5241-5247.1988"xsd:string |
| http://purl.uniprot.org/citations/3141383 | http://purl.uniprot.org/core/author | "Kessler E."xsd:string |
| http://purl.uniprot.org/citations/3141383 | http://purl.uniprot.org/core/author | "Kessler E."xsd:string |
| http://purl.uniprot.org/citations/3141383 | http://purl.uniprot.org/core/author | "Safrin M."xsd:string |
| http://purl.uniprot.org/citations/3141383 | http://purl.uniprot.org/core/author | "Safrin M."xsd:string |
| http://purl.uniprot.org/citations/3141383 | http://purl.uniprot.org/core/date | "1988"xsd:gYear |
| http://purl.uniprot.org/citations/3141383 | http://purl.uniprot.org/core/date | "1988"xsd:gYear |
| http://purl.uniprot.org/citations/3141383 | http://purl.uniprot.org/core/name | "J. Bacteriol."xsd:string |
| http://purl.uniprot.org/citations/3141383 | http://purl.uniprot.org/core/name | "J. Bacteriol."xsd:string |
| http://purl.uniprot.org/citations/3141383 | http://purl.uniprot.org/core/pages | "5241-5247"xsd:string |
| http://purl.uniprot.org/citations/3141383 | http://purl.uniprot.org/core/pages | "5241-5247"xsd:string |
| http://purl.uniprot.org/citations/3141383 | http://purl.uniprot.org/core/title | "Synthesis, processing, and transport of Pseudomonas aeruginosa elastase."xsd:string |
| http://purl.uniprot.org/citations/3141383 | http://purl.uniprot.org/core/title | "Synthesis, processing, and transport of Pseudomonas aeruginosa elastase."xsd:string |
| http://purl.uniprot.org/citations/3141383 | http://purl.uniprot.org/core/volume | "170"xsd:string |
| http://purl.uniprot.org/citations/3141383 | http://purl.uniprot.org/core/volume | "170"xsd:string |
| http://purl.uniprot.org/citations/3141383 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/3141383 |
| http://purl.uniprot.org/citations/3141383 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/3141383 |
| http://purl.uniprot.org/citations/3141383 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/3141383 |
| http://purl.uniprot.org/citations/3141383 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/3141383 |
| http://purl.uniprot.org/uniprot/P14756 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/3141383 |
| http://purl.uniprot.org/uniprot/P14756#attribution-BA214EA7B4E0D3FBC6A1480702E99AF0 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/3141383 |