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Polyamines, ribonucleases, and the stability of RNA

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Summary

The polyamines influence the activity of many enzymes involved in the synthesis and degradation of RNA. These organic cations (putrescine, spermidine, spermine) stimulate, for example, many DNA-dependent RNA polymerases and affect both RNA chain elongation and initiation. The polyamines also bind to polynucleotides, forming complexes having, in many cases, physical properties quite distinct from the parent polymer. Some of these complexes are resistent to ribonuclease mediated hydrolysis. However, polyamines alter the activity, as well as the specificity of some RNases, so the actual rate of breakdown of RNA is dependent on the interaction of polyamine with both RNA and enzyme. The hydrolytic rate may also be controlled by the presence of purine homopolymer, which acts to strongly inhibit RNase activity. The addition of polyadenylic acid tracts to the 3′ terminus of the RNA substrate, for example, protects the unpolyadenylated portion of the RNA molecule from degradation. Longer segments of poly(A) are more effective in this respect; however, regardless of poly(A) length, low concentrations of spermidine reverse the inhibition of RNase activity, with concomitant rapid degradation of the unpolyadenylated portion of the RNA molecule. Thus, RNA degradation depends not only on the presence of RNase, but on poly(A) length and spermidine concentration as well. Although the relative importance, within the cell, of each of these interactions is not known, the above mechanisms illustrate certain of the complexities and interrelations that may exist for the synthesis and, in particular, the RNase mediated degradation of RNA.

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  1. Enzymology and Drug Metabolism Section, Laboratory of Molecular Biology, Baltimore Cancer Research Center, National Cancer Institute, NIH, 21211, Baltimore, Maryland, USA

    T. P. Karpetsky, P. A. Hieter, J. J. Frank & C. C. Levy

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Karpetsky, T.P., Hieter, P.A., Frank, J.J. et al. Polyamines, ribonucleases, and the stability of RNA. Mol Cell Biochem 17, 89–99 (1977). https://doi.org/10.1007/BF01743432

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