PHOSPHORYLATION OF RIBOSOMAL-PROTEIN L30 AFTER HERPES-SIMPLEX VIRUS TYPE-1 INFECTION

In addition to an irreversible stimulation of S6 ribosomal protein pho sphorylation, there is a modification of a subset of ribosomal protein s by phosphorylation after herpes simplex virus type 1 (HSV-1) infecti on. Moreover, in the course of this infection, three additional phosph orylated proteins can be extracted from ribosomes and separated by two -dimensional electrophoresis (2-DE) of total ribosomal proteins. One o f them exhibits an identical molecular mass to L30, while being more a cidic. This protein is phosphorylated on serine residues. The kinetics of appearance of this protein in the ribosomal fraction correlated wi th a decrease in L30 staining, as shown by 2-DE. Determination of the N-terminal amino acid sequence of this extra phosphoprotein and of L30 -derived peptides demonstrated the identity of these two proteins.