Turnover rates of phosphoryl groups in ribosomal proteins of Physarum polycephalum. Evidence for two different mechanisms.

The rate of phosphate exchange in individual ribosomal proteins of Physarum polycephalum was determined in vivo. It was observed that the phosphoryl groups of S3, the major phosphoprotein, had a turnover rate of 1.5% per minute. The phosphoryl groups of proteins L1, L20 and L24 were stable. These results show that the phosphorylation of ribosomal proteins is regulated by at least two different mechanisms. The rapid turnover of phosphoryl groups of the major phosphoprotein is in agreement with the general observation that the phosphate content of this protein is modulated by the physiological state of the cells and possibly involved in the regulation of ribosome activity. The absence of phosphate exchange in acidic proteins suggests that these groups could play a structural role in the ribosome functions.