Mutations in the lipid A deacylase PagL which release the enzyme from its latency affect the ability of PagL to interact with lipopolysaccharide in Salmonella enterica serovar Typhimurium.
PagL, a lipid A deacylase, is unique in that it is latent in the outer membrane of Salmonella enterica serovar Typhimurium. Several point mutations in the extracellular loops of PagL, which do not affect its enzymatic activity, release it from this latency. Precipitation analysis revealed that latent wild-type PagL associated with lipopolysaccharide, but non-latent PagL mutants did not. In contrast, non-latent PagL mutants preferentially associated with some membrane proteins. Precipitation analysis using inactive PagL mutants demonstrated that membrane lipid A deacylation did not affect association. These results indicate that mutations in the lipid A deacylase PagL which relieve the enzyme from its latency affect the ability of PagL to interact with lipopolysaccharide.
Manabe
Takayuki
T
Faculty of Pharmaceutical Sciences, Doshisha Women's College, Kyotanabe, Kyoto 610-0395, Japan.
Kawano
Miyuki
M
Kawasaki
Kiyoshi
K
D000107:Acetylation; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D002265:Carboxylic Ester Hydrolases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008070:Lipopolysaccharides / Q000378:metabolism*; D008969:Molecular Sequence Data; D017354:Point Mutation; D017433:Protein Structure, Secondary; D012486:Salmonella typhimurium / Q000235:genetics
D001426:Bacterial Proteins; D008070:Lipopolysaccharides; D002265:Carboxylic Ester Hydrolases; C424702:PagL protein, Salmonella typhimurium