Effect of phosphorylation on the affinity of acidic proteins from Saccharomyces cerevisiae for the ribosomes.

Electrofocusing of the acidic proteins extracted from Saccharomyces cerevisiae ribosomes shows the presence of eight bands in the gels, which upon treatment with alkaline phosphatase are reduced to three. Two of them, proteins L44 and L45, correspond to the proteins equivalent to the bacterial L7 and L12 and the third, protein Ax, behaves like a supernatant factor. In the ribosome, proteins L44 and L45 are found unphosphorylated and monophosphorylated while protein Ax is detected mostly in a modified state, showing from one to three phosphate groups per molecule. In the cytoplasm where protein Ax is abundant and proteins L44 and L45 are present in small quantities, the three proteins are unphosphorylated. Protein Ax, having one or two phosphate groups, can be removed from the ribosomes in conditions that release the initiation factors, while the triphosphorylated molecules are tightly bound to the particles. The data indicate a relationship between the degree of phosphorylation of protein Az and its affinity for the ribosome.