| http://purl.uniprot.org/citations/24214941 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/24214941 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/24214941 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/24214941 | http://www.w3.org/2000/01/rdf-schema#comment | "Archaea produce membrane lipids that typically possess fully saturated isoprenoid hydrocarbon chains attached to the glycerol moiety via ether bonds. They are functionally similar to, but structurally and biosynthetically distinct from, the fatty acid-based membrane lipids of bacteria and eukaryotes. It is believed that the characteristic lipid structure helps archaea survive under severe conditions such as extremely low or high pH, high salt concentrations, and/or high temperatures. We detail here the first successful production of an intact archaeal membrane lipid, which has fully saturated isoprenoid chains, in bacterial cells. The introduction of six phospholipid biosynthetic genes from a methanogenic archaeon, Methanosarcina acetivorans, in Escherichia coli enabled the host bacterium to synthesize the archaeal lipid, i.e., diphytanylglyceryl phosphoglycerol, while a glycerol modification of the phosphate group was probably catalyzed by endogenous E. coli enzymes. Reduction of the isoprenoid chains occurred only when archaeal ferredoxin was expressed with geranylgeranyl reductase, suggesting the role of ferredoxin as a specific electron donor for the reductase. This report is the first identification of a physiological reducer for archaeal geranylgeranyl reductase. On the other hand, geranylgeranyl reductase from the thermoacidophilic archaeon Sulfolobus acidocaldarius could, by itself, replace both its orthologue and ferredoxin from M. acetivorans, which indicated that an endogenous redox system of E. coli reduced the enzyme."xsd:string |
| http://purl.uniprot.org/citations/24214941 | http://purl.org/dc/terms/identifier | "doi:10.1128/jb.00927-13"xsd:string |
| http://purl.uniprot.org/citations/24214941 | http://purl.org/dc/terms/identifier | "doi:10.1128/jb.00927-13"xsd:string |
| http://purl.uniprot.org/citations/24214941 | http://purl.uniprot.org/core/author | "Hemmi H."xsd:string |
| http://purl.uniprot.org/citations/24214941 | http://purl.uniprot.org/core/author | "Hemmi H."xsd:string |
| http://purl.uniprot.org/citations/24214941 | http://purl.uniprot.org/core/author | "Isobe K."xsd:string |
| http://purl.uniprot.org/citations/24214941 | http://purl.uniprot.org/core/author | "Isobe K."xsd:string |
| http://purl.uniprot.org/citations/24214941 | http://purl.uniprot.org/core/author | "Ogawa T."xsd:string |
| http://purl.uniprot.org/citations/24214941 | http://purl.uniprot.org/core/author | "Ogawa T."xsd:string |
| http://purl.uniprot.org/citations/24214941 | http://purl.uniprot.org/core/author | "Yoshimura T."xsd:string |
| http://purl.uniprot.org/citations/24214941 | http://purl.uniprot.org/core/author | "Yoshimura T."xsd:string |
| http://purl.uniprot.org/citations/24214941 | http://purl.uniprot.org/core/author | "Yokoi T."xsd:string |
| http://purl.uniprot.org/citations/24214941 | http://purl.uniprot.org/core/author | "Yokoi T."xsd:string |
| http://purl.uniprot.org/citations/24214941 | http://purl.uniprot.org/core/author | "Hirose K."xsd:string |
| http://purl.uniprot.org/citations/24214941 | http://purl.uniprot.org/core/author | "Hirose K."xsd:string |
| http://purl.uniprot.org/citations/24214941 | http://purl.uniprot.org/core/date | "2014"xsd:gYear |
| http://purl.uniprot.org/citations/24214941 | http://purl.uniprot.org/core/date | "2014"xsd:gYear |
| http://purl.uniprot.org/citations/24214941 | http://purl.uniprot.org/core/name | "J. Bacteriol."xsd:string |
| http://purl.uniprot.org/citations/24214941 | http://purl.uniprot.org/core/name | "J. Bacteriol."xsd:string |
| http://purl.uniprot.org/citations/24214941 | http://purl.uniprot.org/core/pages | "417-423"xsd:string |
| http://purl.uniprot.org/citations/24214941 | http://purl.uniprot.org/core/pages | "417-423"xsd:string |
| http://purl.uniprot.org/citations/24214941 | http://purl.uniprot.org/core/title | "Geranylgeranyl reductase and ferredoxin from Methanosarcina acetivorans are required for the synthesis of fully reduced archaeal membrane lipid in Escherichia coli cells."xsd:string |