In vivo inhibition of glutamine synthetase induces sporulation in a protease deficient asporogenous mutant of Bacillus polymyxa.

In vivo inhibition of glutamine synthetase (GS) by l-methionine sulfoximine induces sporulation in a protease deficient mutant of Bacillus polymyxa. This induction of sporulation is accompanied by derepression of EDTA insensitive proteases(s) which seems to be specific for differentiation. Some amino acid analogues derepress proteolytic activity without inducing sporulation, but these proteases are sensitive to metal chelators like those in the vegetative cells. When the proteolytic activity is restored, the mutant cells, which are smaller than the parental strain, regain their normal size. [ABSTRACT FROM AUTHOR]