PMID: 108259May 1, 1979

Role of heme in synthesis and membrane binding of succinic dehydrogenase in Bacillus subtilis

Journal of Bacteriology
E HolmgrenL Rutberg

Abstract

A 5-aminolevulinic acid-requiring mutant of Bacillus subtilis was isolated. When the mutant is shifted from medium containing 5-aminolevulinic acid to medium lacking this growth factor, the bacteria continued to grow at undiminished rate for about three generations. The membranes from these bacteria contained severely reduced amounts of cytochrome. The mutant was used to study the role of heme synthesis on synthesis and membrane binding of succinic dehydrogenase (SDH). The amount of SDH in whole-cell lysates in the soluble cytoplasmic fraction and in membranes was determined by one-dimensional (rocket) immunoelectrophoresis with an SDH-specific antiserum. After heme synthesis was blocked, the relative amount of SDH in the membrane decreased, whereas increasing amounts of SDH antigen were found in the cytoplasm. When heme synthesis was resumed on readdition of 5-aminolevulinic acid, the amount of membrane-bound SDH antigen increased at a much faster rate than net synthesis. During a 3-h growth period without 5-aminolevulinic acid, there was little change in the pattern of membrane proteins as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis of radioactively labeled membranes, as compared to membranes from ...Continue Reading

Related Concepts

Aminolevulinic Acid Hydrochloride
Natto Bacteria
Bacterial Proteins
Plasma Membrane
Heme
Cell Surface Proteins
Peptide Biosynthesis
Plasma Protein Binding Capacity
Succinate Dehydrogenase

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