SUMMARY: Under sporulation conditions, mutant SE63 secreted into the medium an inhibitor of the extracellular DNAase that is specifically associated with stage II to III of sporulation. The inhibitor was a heat-labile protein with a molecular weight of 18000–20000. A cell-bound, presumably intracellular, inhibitor with the same properties was found in extracts of wild-type cells and of the mutant. The mechanisms by which the mutation, designated , might cause the secretion of a protein that is normally intracellular are discussed. The mutation was mapped by transduction with phage PBS1 and it lies between and It was also introduced into a variety of sporulation mutants including some blocked at the earliest known stages of the process. In all of these it caused secretion of the inhibitor. It is concluded that the secretion is therefore not integrally associated with sporulation but is, instead, part of the response of the cells to the nutritional step-down conditions in which spore formation is induced.


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