The storage of globin mRNA during the inhibition of protein synthesis by heme deprivation.
The inhibition of protein synthesis in reticulocytes and their lysates caused by heme-deprivation is reversible on restoration of an optimal heme concentration. Inhibition is accompanied by the disaggregation of polyribosomes and the accumulation of components of the translational mechanism. By determining the fate of labeled globin 9S mRNA added to an unfractionated reticulocyte lysate cell-free system, we find that normal cellular mRNA accumulates during inhibition in 20S and 48S complexes and in a complex which sediments just ahead of the 80S ribosome dimer OD260 peak (designated as greater than or equal to 80S complex)1. The 20S and greater than 80S complexes are the major pools of stored mRNA which is readily translated if optimal heme conditions are restored. In the 48S complex, however, the mRNA remains non-functional, and the complex is abortive, probably as a result of deacylation of the Met.tRNAf.
D000818:Animals; D002474:Cell-Free System; D005914:Globins / Q000235:genetics / Q000378:metabolism*; D006418:Heme / Q000172:deficiency*; D011132:Polyribosomes / Q000378:metabolism; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000378:metabolism*; D011817:Rabbits; D012156:Reticulocytes / Q000378:metabolism
D012333:RNA, Messenger; D006418:Heme; D005914:Globins