Polyribosomal structures inactive for protein synthesis present in erythroid cells during terminal stages of differentiation.
During the terminal stages of differentiation nucleated erythroid cells from the fetal mouse synthesize hemoglobin at a lower rate because after the last cycle of cell division about half of their polyribosomal structures are rendered inactive for protien synthesis though they maintain their aggregated shape. Partially inactive polyribosomes are tested in comparison with normal polyribosomes for the capacity to support polypeptide chain synthesis in cell-free conditions. The following observations are made: a) no difference is found for the profile on sucrose density gradients; b) partially inactive polyribosomes carry growing polypeptide chains in reduced amounts in comparison with active polyribosomes; c) partially inactive polyribosomes are not capable to release "run off" 80 S ribosomal monomers and to dissociate to active ribosomal subunits. These data are interpreted as the evidence for a block of chain termination producing inactivation of polyribosomes during the late maturation of nucleated erythroid cells.
D000818:Animals; D002454:Cell Differentiation; D002499:Centrifugation, Density Gradient; D004912:Erythrocytes / Q000378:metabolism* / Q000648:ultrastructure; D005260:Female; D005333:Fetus; D006454:Hemoglobins / Q000096:biosynthesis*; D051379:Mice; D011072:Poly U; D011132:Polyribosomes / Q000378:metabolism*; D014176:Protein Biosynthesis; D012270:Ribosomes / Q000378:metabolism / Q000648:ultrastructure; D014817:Vitelline Membrane / Q000378:metabolism
D006454:Hemoglobins; D011072:Poly U