%0 Journal Article %A Jenkinson, H. F. %A Lord, H. %T Protease Deficiency and Its Association with Defects in Spore Coat Structure, Germination and Resistance Properties in a Mutant of Bacillus subtilis %D 1983 %J Microbiology, %V 129 %N 9 %P 2727-2737 %@ 1465-2080 %R https://doi.org/10.1099/00221287-129-9-2727 %I Microbiology Society, %X Spores formed by Bacillus subtilis carrying the mutation ger-36 are lysozyme-sensitive and germination-defective. The coats of these spores lack a number of polypeptides normally found in the spore coat, and four additional polypeptides are present that are not normally found in the coats of wild-type spores. The ger-36 mutation also prevents the synthesis (at about stage V) and the incorporation into the spore outer layers, of an intracellular protease (protease B, approx. mol wt. of monomer 25000). A partial revertant of a strain carrying ger-36 was isolated and this had an additional mutation in a locus distinct from gerE. The suppressing mutation restored the protease activity, but not the germination defect. It partly restored resistance to lysozyme and the spores formed had apparently normal coat protein composition except for the absence of one polypeptide (mol wt. 36000). %U https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-129-9-2727