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http://purl.uniprot.org/citations/10048027http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10048027http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10048027http://www.w3.org/2000/01/rdf-schema#comment"The suppressor mutation, named sfhC21, that allows Escherichia coli ftsH null mutant cells to survive was found to be an allele of fabZ encoding R-3-hydroxyacyl-ACP dehydrase, involved in a key step of fatty acid biosynthesis, and appears to upregulate the dehydrase. The ftsH1(Ts) mutation increased the amount of lipopolysaccharide at 42 degrees C. This was accompanied by a dramatic increase in the amount of UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase [the IpxC (envA) gene product] involved in the committed step of lipid A biosynthesis. Pulse-chase experiments and in vitro assays with purified components showed that FtsH, the AAA-type membrane-bound metalloprotease, degrades the deacetylase. Genetic evidence also indicated that the FtsH protease activity for the deacetylase might be affected when acyl-ACP pools were altered. The biosynthesis of phospholipids and the lipid A moiety of lipopolysaccharide, both of which derive their fatty acyl chains from the same R-3-hydroxyacyl-ACP pool, is regulated by FtsH."xsd:string
http://purl.uniprot.org/citations/10048027http://purl.org/dc/terms/identifier"doi:10.1046/j.1365-2958.1999.01221.x"xsd:string
http://purl.uniprot.org/citations/10048027http://purl.org/dc/terms/identifier"doi:10.1046/j.1365-2958.1999.01221.x"xsd:string
http://purl.uniprot.org/citations/10048027http://purl.uniprot.org/core/author"Inoue K."xsd:string
http://purl.uniprot.org/citations/10048027http://purl.uniprot.org/core/author"Inoue K."xsd:string
http://purl.uniprot.org/citations/10048027http://purl.uniprot.org/core/author"Fierke C.A."xsd:string
http://purl.uniprot.org/citations/10048027http://purl.uniprot.org/core/author"Fierke C.A."xsd:string
http://purl.uniprot.org/citations/10048027http://purl.uniprot.org/core/author"Jackman J.E."xsd:string
http://purl.uniprot.org/citations/10048027http://purl.uniprot.org/core/author"Jackman J.E."xsd:string
http://purl.uniprot.org/citations/10048027http://purl.uniprot.org/core/author"Raetz C.R."xsd:string
http://purl.uniprot.org/citations/10048027http://purl.uniprot.org/core/author"Raetz C.R."xsd:string
http://purl.uniprot.org/citations/10048027http://purl.uniprot.org/core/author"Matsuzawa H."xsd:string
http://purl.uniprot.org/citations/10048027http://purl.uniprot.org/core/author"Matsuzawa H."xsd:string
http://purl.uniprot.org/citations/10048027http://purl.uniprot.org/core/author"Ogura T."xsd:string
http://purl.uniprot.org/citations/10048027http://purl.uniprot.org/core/author"Ogura T."xsd:string
http://purl.uniprot.org/citations/10048027http://purl.uniprot.org/core/author"Young K."xsd:string
http://purl.uniprot.org/citations/10048027http://purl.uniprot.org/core/author"Young K."xsd:string
http://purl.uniprot.org/citations/10048027http://purl.uniprot.org/core/author"Tatsuta T."xsd:string
http://purl.uniprot.org/citations/10048027http://purl.uniprot.org/core/author"Tatsuta T."xsd:string
http://purl.uniprot.org/citations/10048027http://purl.uniprot.org/core/author"Coleman J."xsd:string
http://purl.uniprot.org/citations/10048027http://purl.uniprot.org/core/author"Coleman J."xsd:string
http://purl.uniprot.org/citations/10048027http://purl.uniprot.org/core/author"Tomoyasu T."xsd:string
http://purl.uniprot.org/citations/10048027http://purl.uniprot.org/core/author"Tomoyasu T."xsd:string