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Science 16 November 1962:
Vol. 138. no. 3542, pp. 810 - 813
DOI: 10.1126/science.138.3542.810
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Articles

Fate of a Synthetic Polynucleotide Directing Cell-Free Protein Synthesis I. Characteristics of Degradation

Samuel H. Barondes 1 and Marshal W. Nirenberg 1

1 National Institutes of Health, Bethesda 14, Maryland

Tritiated-polyuridylie acid was degraded rapidly in extracts of Escherichia coli and degradation was not dependent on concomitant polyphenylalanine synthesis. Since a large portion of the polymer was degraded before appreciable polyphenylalanine was synthesized, the catalytic activity of the undegraded polyuridylic acid in directing protein synthesis was suggested. The predominant breakdown products were 5'-mononucleotide phosphates. Possible enzymatic routes of polyuridylic acid breakdown are discussed.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Protein Biosynthesis: Some Alternative Considerations on the Current Hypothesis.
R. W. Hendler (1963)
Science 142, 402-405
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Coding Ambiguity in Cell-Free Extracts of Chlamydomonas.
R. Sager, I. B. Weinstein, and Y. Ashkenazi (1963)
Science 140, 304-306
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Hemoglobin and Polyphenylalanine Synthesis with Reticulocyte Ribosomes.
B. Hardesty, R. Arlinghaus, J. Shaeffer, and R. Schweet (1963)
Cold Spring Harb Symp Quant Biol 28, 215-222
   Abstract »    PDF »
Polyribosomes Active in Reticulocyte Protein Synthesis.
P. A. Marks, E. R. Burka, R. Rifkind, and D. Danon (1963)
Cold Spring Harb Symp Quant Biol 28, 223-226
   Abstract »    PDF »
The Structure and Function of Polyribosomes.
A. Rich, J. R. Warner, and H. M. Goodman (1963)
Cold Spring Harb Symp Quant Biol 28, 269-285
   Abstract »    PDF »


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Science. ISSN 0036-8075 (print), 1095-9203 (online)