Hans J. Rhaese

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Bacillus subtilis contains an enzyme that synthesizes the highly phosphorylated nucleotide adenosine 5',3'(2')-bis(triphosphate), abbreviated p(3)Ap(3). This enzyme can be demonstrated to be present in the cytoplasmic membrane of B. subtilis at all stages of growth and development. During vegetative growth its enzymatic activity is inhibited by(More)
A model explaining the mechanism of initiation of differentiation is presented. It is based on the finding that sporulation in B. subtilis can be induced by the same nutrient deficiencies that also induce the synthesis of highly phosphorylated nucleotides. Two of these nucleotides are synthesized by membrane vesicles. Synthesis can be inhibited by the same(More)
To test our model on the mechanism of initiation of differentiation in Bacillus subtilis, we tested early blocked (stage 0) sporulation mutants for their ability to synthesize highly phosphorylated nucleotides. We also isolated early blocked asporogenous mutants with the aid of the intercalating drug tilorone. Among all mutants tested we found that the(More)
Membrane proteins from vegetative and sporulating cells of Bacillus subtilis were separated by the two-dimensional gel electrophoresis system using isoelectric focusing and sodium dodecyl sulfate/polyacrylamide gel electrophoresis (O'Farrell technique). Membrane proteins were isolated according to published procedures. The gels were stained with Coomassie(More)