Secretion of proteins by Bacillus subtilis 168 grown in the presence of membrane active agents (alcohols).
Sodium dodecyl sulphate-polyacrylamide gel electrophoresis was used to study the composition of proteins secreted by the Gram-positive microorganism Bacillus subtilis strain 168 when the latter was grown in the presence of primary alcohols (methanol, ethanol, 1-propanol and 1-butanol). These membrane-active agents had different effects on the pattern of proteins exported by B. subtilis. The secretion of some proteins was inhibited by the alkanols while that of others was stimulated, depending on the type of drug used. All alcohols were found to decrease the activity of extracellular enzymes such as alpha-amylase and serine protease without affecting significantly the activity of these enzymes when tested in vitro. The observed effects might be due to the ability of these agents to perturb the structure of biological membranes, thus interfering with the process of protein translocation through the lipid bilayers.
D000438:Alcohols / Q000494:pharmacology*; D001412:Bacillus subtilis / Q000378:metabolism*; D001426:Bacterial Proteins / Q000032:analysis / Q000096:biosynthesis*; D004591:Electrophoresis, Polyacrylamide Gel; D012697:Serine Endopeptidases / Q000302:isolation & purification; D012967:Sodium Dodecyl Sulfate
D000438:Alcohols; D001426:Bacterial Proteins; D012967:Sodium Dodecyl Sulfate; D012697:Serine Endopeptidases