Defects in the nutrient-dependent methylation of a membrane-associated protein in spo mutants of Bacillus subtilis.

Methylation of a membrane-associated protein with an apparent molecular mass of 40,000 daltons has been observed in Bacillus subtilis. The methylation was nutrient dependent and occurred with a doubling time of 4 +/- 1 min. In wild-type strains, the half-life of turnover of the methyl group(s) was 17 +/- 6 min. Several isogenic strains of B. subtilis containing spo0 mutations (spo0A and spo0H) were found to be normal in glutamate-dependent methylation of the protein and turnover of the methyl group(s). In strains containing spo0B and spo0E mutations, the methyl group(s) were incorporated in response to glutamate addition but turnover was not at a normal rate. The half-life of methyl group turnover was extended to 45 +/- 3 min in these strains. In a spo0K mutant and in spoIIJ and spoIIF mutants, the protein was not significantly methylated. The methylation of a 40,000 dalton protein was also found to be dependent on phosphate. This methylation was observed in wild-type and spo0A and spo0H strains with a doubling time of 4 +/- 1 min and a half-life of turnover of the methyl group(s) of 11 +/- 3 min. In strains containing spo0B, spo0E, and spo0F mutations, the phosphate-dependent incorporation of the methyl group(s) was normal (5 +/- 1 min) but the turnover half-life was extended to 46 +/- 8 min. It is not known whether the nitrogen-dependent and phosphate-dependent systems methylated the same protein.(ABSTRACT TRUNCATED AT 250 WORDS)