PMID:10048027
| Citation |
Ogura, T, Inoue, K, Tatsuta, T, Suzaki, T, Karata, K, Young, K, Su, LH, Fierke, CA, Jackman, JE, Raetz, CR, Coleman, J, Tomoyasu, T and Matsuzawa, H (1999) Balanced biosynthesis of major membrane components through regulated degradation of the committed enzyme of lipid A biosynthesis by the AAA protease FtsH (HflB) in Escherichia coli. Mol. Microbiol. 31:833-44 |
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| Abstract |
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. |
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| Keywords |
ATP-Dependent Proteases; Amidohydrolases/analysis; Amidohydrolases/physiology; Bacterial Proteins/genetics; Bacterial Proteins/physiology; Blotting, Western; Cell Membrane/ultrastructure; Escherichia coli/enzymology; Escherichia coli Proteins; Gene Expression Regulation, Bacterial; Genotype; Lipid A/biosynthesis; Lipopolysaccharides/analysis; Membrane Proteins/genetics; Membrane Proteins/physiology; Microscopy, Electron; Models, Biological; Mutagenesis; Phenotype; Precipitin Tests; Temperature; Time Factors |
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