Abstract
Glycerol permeation was studied in B. subtilis 168 trp gl+ and its two mutants gl1 and gl2. The mutant gl1 has all the enzymes required for the degradation of endocellular glycerol. The mutant gl2 is impaired in the enzyme glycerol kinase. In the presence of increasing concentrations of glycerol-14C, incorporation of radioactivity by the wild strain obeys Michaelis law while it is linear in the case of the mutant gl1. Thus the mutant gl1 is cryptic towards glycerol. No evidence was found as to the formation of an intracellular pool of glycerol in any of the three strains (gl+, gl1, gl2) studied. This result suggests that permeation of glycerol in B. subtilis is probably facilitated by diffusion. Sporulation of the mutant gl1 in presence of glycerol is explained by a mutation affecting the permeation system. Thus glycerol enters in the mutant cells by simple diffusion. As a consequence, the metabolism is greatly reduced and the sporulation mechanism is triggered.

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