Eucaryotic oligonucleotides affecting mRNA translation |
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Authors: | Sylvia Lee-Huang Jose Manuel Sierra Ramon Naranjo Witold Filipowicz Severo Ochoa |
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Institution: | 1. Department of Biochemistry, New York University School of Medicine, New York, New York, 10016 USA;2. Roche Institute of Molecular Biology, Nutley, New Jersey 07110 USA |
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Abstract: | High speed-supernatants and ribosomal salt washes of dormant and developing Artemia salina embryos contain a potent inhibitor of translation; it blocks the elongation factor EF-1-dependent ribosomal binding of aminoacyl-tRNA. A translation activator that counteracts the effect of the inhibitor is found in the same fractions from developing embryos; there is little activator in undeveloped cysts. The appearance of the activator may be responsible for the onset of protein synthesis when development resumes. Both compounds are oligonucleotides. The inhibitor, Mr about 6000, is rich in pyrimidines (47% U, 11% A, 26% C, 16% G), sensitive to RNase A, and resistant to RNase T1. The activator, Mr about 9000, is rich in guanine (33% U, 10% A, 6% C, 51% G), sensitive to RNase T1, and resistant to RNase A. It complexes with the inhibitor and inactivates it. Inhibitor and activator seem to be end products of hydrolysis of embryo RNA by RNase T1 and RNase A, respectively, and ribosomal salt washes of developing embryos have higher RNase A activity than corresponding fractions from dormant cysts. |
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