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Influence of Testosterone and Polyuridylic Acid on the Incorporation of Phenylalanine into Peptide Linkage by Prostatic Ribosomes

Naturevolume 199pages808809 (1963) | Download Citation

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Abstract

RECENT studies1 on the transfer of radioactivity from soluble ribonucleic acid-(sRNA)-valine-14C to protein-like material by isolated prostatic ribosomes suggested that the levels of template RNA associated with these particles are controlled by testicular hormones. In line with this conclusion was the observation that randomly ordered copolymers of uridylic and guanylic acids (poly UG) stimulated valine incorporation by prostatic ribosomes from orchiectomized animals to a much greater extent than was found with ribosomes prepared from castrates which were treated with testosterone. However, two considerations complicate interpretation of the response of cell-free valine incorporating systems to poly UG. First, poly UG (prepared by the action of polynucleotide phosphorylase on a mixture of uridine and guanosine diphosphates) represents a complex mixture of polyribonucleotides of varying size and base sequences, the exact composition of which is difficult to ascertain. Secondly, the effects of guanine-containing polyribonucleotides on ribosomal amino-acid incorporating systems seem to depend not only on the base compositions of the polymers, but also on the degree of ordered secondary structure which they may exhibit in solution2. It became of interest, therefore, to examine the response of prostatic ribosomes to polyribonucleotides containing only one base. It is well established that polyuridylic acid (poly U) directs the entry of phenylalanine into peptide linkage in the presence of ribosomes from a number of tissues3–8. The following experiments concern factors which influence the transfer of radioisotope from sRNA-phenylalanine-14C to acid-insoluble products by prostatic ribosomes, incubated in the absence and presence of poly U.

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References

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    Liao, S., and Williams-Ashman, H. G., Proc. U.S., Nat. Acad. Sci., 48, 1956 (1962).

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    Fessenden, J. M., Cairncross, J., and Moldave, K., Proc. U.S. Nat. Acad. Sci., 49, 82 (1963).

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    Arnstein, H. R. V., Cox, R. A., and Hunt, J. A., Nature, 194, 1042 (1962).

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Affiliations

  1. Ben May Laboratory for Cancer Research, and Department of Biochemistry, University of Chicago

    • D. A. SILVERMAN
    • , SHUTSUNG LIAO
    •  & H. G. WILLIAMS-ASHMAN

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https://doi.org/10.1038/199808a0

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