SUMMARY: Forespores of 60015 were isolated from sporulating cells at and were incubated with an amino acid mixture containing [C]phenylalanine. Three species of C-labelled cytoplasmic proteins synthesized in the forespores were purified to homogeneity by gel filtration in the presence of detergents and by ion-exchange chromatography. The molecular weights of the purified proteins, called A, B and C, were estimated by SDS-PAGE as 24200, 11500 and 12700, respectively. Protein B contained remarkably high amounts of tyrosine (23.8%) and alanine (22.8%), and proteins A and C contained relatively high amounts of glutamate + glutamine, glycine, and alanine (10.4 to 13.3%). The synthesis of these proteins can provide markers for the control events in the forespore compartment during sporulation.


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