Coordinate regulation of polypeptide chain initiation and elongation in rabbit reticulocytes.
Under normal conditions, reticulocytes synthesize alpha- and beta-globin polypeptides at equal rates. Incubation in the absence of hemin or under anoxia or hypertonic stress (100 mM excess NaCl) reduces the rate of protein synthesis to 30-50% of control levels. However, only hemin deprivation causes a reduction in polyribosome size and preferential inhibition of alpha-globin synthesis consistent with specific reduction in the rate of polypeptide chain initiation. Polyribosomal profiles are unaffected by anoxic or hypertonic stress and the ratio of alpha:beta globin synthesis remains close to unity. Measurement of ribosome transit time indicates that anoxic or hypertonic stress causes a decrease in the rate of polypeptide chain elongation that varies with the degree of inhibition of protein synthesis. Ribosomes isolated from stressed cells exhibit a reduced ability to bind 35S-met-tRNAf, suggesting that the ability to form initiation complexes is also impaired. These results suggest that reticulocytes, unlike nucleated cell lines, can coordinately reduce rates of initiation and elongation in response to certain physiological stresses.
D000818:Animals; D001798:Blood Proteins / Q000096:biosynthesis; D005914:Globins / Q000096:biosynthesis; D006427:Hemin / Q000172:deficiency; D000860:Hypoxia / Q000378:metabolism; D008297:Male; D010441:Peptide Chain Elongation, Translational; D010442:Peptide Chain Initiation, Translational; D011132:Polyribosomes / Q000378:metabolism; D012156:Reticulocytes / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism; D012462:Saline Solution, Hypertonic; D013312:Stress, Physiological / Q000378:metabolism; D013997:Time Factors
D001798:Blood Proteins; D012462:Saline Solution, Hypertonic; D006427:Hemin; D005914:Globins