Suppression of temperature-sensitive sporulation of a Bacillus subtilis elongation factor G mutant by RNA polymerase mutations.
A class of rifampin-resistant (rfm) mutations of Bacillus subtilis suppresses the temperature-sensitive sporulation of a fusidic acid-resistant mutant. FUS426, which has an altered elongation factor G. The rfm mutation suppressed only the sporulation defect caused by the elongation factor G mutation, but could not suppress other types of induced sporulation defects. Genetic and biochemical analyses showed that the sporulation suppression by the rfm mutation was caused by a single mutation in RNA polymerase. After the early sporulation phase, the apparent rate of RNA synthesis of FUS426, measured by [3H]uracil or [3H]uridine incorporation into RNA, became lower than that of the wild-type strain, and this decrease was reversed by the rfm mutation. However, when the total rate of RNA synthesis of FUS426 was calculated by measuring the specific activity of [3H]UTP and [3H]CTP, it was higher than that of the rfm mutant, RIF122FUS426. The possible mechanism of the functional interaction between elongation factor G and RNA polymerase during sporulation is discussed.
D001412:Bacillus subtilis / Q000235:genetics / Q000502:physiology*; D012321:DNA-Directed RNA Polymerases / Q000502:physiology*; D005796:Genes; D009154:Mutation; D010445:Peptide Elongation Factors / Q000502:physiology*; D012329:RNA, Bacterial / Q000096:biosynthesis; D012335:RNA, Ribosomal / Q000096:biosynthesis; D013171:Spores, Bacterial; D013696:Temperature; D014544:Uridine Triphosphate / Q000378:metabolism
D010445:Peptide Elongation Factors; D012329:RNA, Bacterial; D012335:RNA, Ribosomal; D012321:DNA-Directed RNA Polymerases; D014544:Uridine Triphosphate