Protein Phosphorylation in Bacillus thuringiensis during Growth and  -Endotoxin Production

Abstract

2559At least 14 phosphopolypeptides in which the phosphate groups were present as mono-esters were detected by pulse labelling of Bacillus thuringiensis subsp. kurstaki HD-1-Dipel with [32P]orthophosphate at different stages of growth and differentiation. Marked changes in the profile of phosphopolypeptides were observed primarily during the late exponential phase of growth. Several phosphopolypeptides co-purified with the endotoxin crystal of this subspecies and the phosphoamino acid residue of the most abundant ( M , 25 000) phosphopolypeptide was identified as phosphothreonine. Comparison of the phosphopolypeptides in endotoxin crystals from several subspecies suggested that M , 25000 species might be a common component.

Membrane-protein phosphorylation in the Bacillus subtilis cell cycle

“…Sporulation-dependent phosphorylation of peptides was found in Bacillus subtilis [5,1 I] and in B. thuringiensis var. kurstaki [15].…”