Characterization of succinic dehydrogenase mutants of Bacillus subtilis by crossed immunoelectrophoresis.
Eleven succinic dehydrogenase (SDH) mutants in Bacillus subtilis were analyzed by crossed immunoelectrophoresis with antiserum prepared against wild-type B. subtilis cytoplasmic membrane. A precipitate which stained for SDH was found in Triton X-100-solubilized wild-type membranes and in membranes from two of the SDH mutants. The remaining nine mutants did not show an SDH-staining precipitate. The respective mutations in these nine mutants all map in one locus, citF (Ohné et al., J. Bacteriol. 115:738-745, 1973). An SDH-specific antiserum was prepared by immunizing rabbits with the SDH precipitate obtained in crossed immunoelectrophoresis with solubilized wild-type membrane. Using this antiserum, it was shown that all of the nine citF mutants lack an SDH-specific antigen in the membrane but five of the citF mutants have a soluble SDH-specific antigen. No major differences were found in sodium dodecyl sulfatepolyacrylamide gels of membrane proteins from wild-type B. subtilis and from SDH mutants. A model for the organization of SDH in B. subtilis is proposed.
D001412:Bacillus subtilis / Q000201:enzymology / Q000235:genetics*; D001426:Bacterial Proteins / Q000032:analysis; D005796:Genes; D007123:Immunoelectrophoresis, Two-Dimensional; D008565:Membrane Proteins / Q000032:analysis; D008954:Models, Biological; D009154:Mutation; D013385:Succinate Dehydrogenase / Q000032:analysis / Q000235:genetics* / Q000378:metabolism
D001426:Bacterial Proteins; D008565:Membrane Proteins; D013385:Succinate Dehydrogenase