Differential protein synthesis during sporulation in the slime mold Physarum polycephalum.

The size distribution and synthesis of polypeptide chains and the polysome patterns were studied during sporulation of the slime mold Physarum polycephalum, and were compared with nonsporulating controls. The proteins were divided into a 27,000 x g supernatant (buffer-soluble proteins) and a pellet (buffer-insoluble proteins) while still native. The sodium dodecyl sulfate complexes of the denatured proteins were separated on polyacrylamide gels containing urea. The following differences were found between sporulating and nonsporulating cultures. (i) The distribution of the soluble proteins into bands from sporulating and control cultures was the same in stained patterns; however, there was a slight shift toward increased synthesis of larger polypeptide chains in the radioactivity patterns of the soluble proteins in sporulating cultures. (ii) The amount of histones in the sporulating cultures was less than 30% of the values in the controls. Also, histone synthesis was reduced to less than 10% of that in the nonsporulating controls. In addition, proteins in three defined regions, corresponding to molecular weights of 70,000 to 75,000 (I), 55,000 (II), and 41,000 (III), were synthesized in sporulating cultures at a rate at least twice that in controls. Polypeptides corresponding to peaks I and II could be extracted from purified walls of mature spores. (iii) The polysome pattern as revealed by sucrose density centrifugation showed a breakdown of heavy polysomes at 3 hr after illumination, with their reappearance 4 hr later. The latter pattern, however, differed from that of the nonsporulating control in that the amount of light polysomes was reduced. This might account for the reduction in histone synthesis.