The translation of the messenger for the poly(A)-binding protein-associated with translated mRNA is suppressed. A case of cytoplasmic repression in duck erythroblasts.
In vivo protein synthesis in duck erythroblasts was compared to in vitro translation of polyribosomal and free cytoplasmic mRNA. The in vivo study showed the absence of de novo synthesis of the Mr 73 000 poly(A)-binding protein found associated with all polyribosomal mRNA. In vitro translation demonstrated that the mRNA for this protein is absent from the polyribosomal mRNA fraction but constitutes a medium frequency messenger among the repressed free mRNA. This result confirms the existence of a qualitative translational control in terminal differentiating duck erythroblasts leading eventually to the arrest of the protein synthesizing machinery.
D000818:Animals; D002352:Carrier Proteins / Q000096:biosynthesis*; D003593:Cytoplasm / Q000378:metabolism*; D004372:Ducks / Q000097:blood; D004900:Erythroblasts / Q000378:metabolism*; D066298:In Vitro Techniques; D039102:Poly(A)-Binding Proteins; D011132:Polyribosomes / Q000378:metabolism; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000097:blood*; D012335:RNA, Ribosomal / Q000097:blood; D012261:Ribonucleoproteins / Q000097:blood
D002352:Carrier Proteins; D039102:Poly(A)-Binding Proteins; D012333:RNA, Messenger; D012335:RNA, Ribosomal; D012261:Ribonucleoproteins; C026452:messenger ribonucleoprotein