Isogenic strains of Bacillus subtilis carrying sup-1 (26), sup-3 (10), or their wild-type alleles were constructed in three genetic backgrounds. The patterns of suppression at 37 and 43.5 C, identity of mapping site, effects of the suppressor genes on growth rate, sporulation, and production of altered enzymes were examined. The similarity of the suppression pattern by sup-1 and sup-3 suggests that the suppressors are of the same type. They do not, however, represent mutations in the same gene, since, based on differences in temperature sensitivity of phage mutants in suppressor-containing hosts, sup-1 and sup-3 insert different amino acids and can coexist within the same cell. The ability to produce slow-migrating forms of enzymes of the type described in the accompanying paper was co-transferred with either of the suppressor genes during transformation, was lost on reversion of the suppressor mutations, and was independent of the genetic background. Similarly, transformation and reversion studies indicate that the additional pleiotropic properties such as slow growth rate and inability to attain competence or to yield plaques with phi105C4, which are characteristic of the Okubo sup-1 strain (HA101B) but not its early sporulation defect, result from the presence of the suppressor mutation. The possible mechanisms by which altered enzyme forms and the additional pleiotropic effects are produced in suppressor strains are discussed. In addition, a newly recognized suppressor phenotype is described and partially characterized.

Amino Acid Oxidoreductases↗

PubMed1974

Altered proteins with triosephosphate isomerase activity in suppressor-containing strains of Bacillus subtilis.

Suppressor mutations in Bacillus subtilis cause the synthesis of a new protein with the enzymatic activity of l-leucine dehydrogenase and two groups of new proteins with the activity of triosephosphate isomerase. The new isoenzymes of triosephosphate isomerase are separable by zone electrophoresis and differ among themselves in elution behavior upon gel permeation chromatography. One group has an apparent average molecular weight of 120,000 to 135,000, which is more than twice that of the wild-type enzyme. Another group appears to be even higher in molecular weight. These data are consistent with the working hypothesis that the new isoenzymes are produced by extension of growing polypeptide chains through one or more chain-terminating triplets, although other mechanisms resulting in alteration of shapes, charges, or associations of the enzymes are not excluded.

Alleles↗

PubMed1973