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image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Molecular and Cellul...arrow_drop_down
image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao
Molecular and Cellular Biochemistry
Article . 1977 . Peer-reviewed
License: Springer TDM
Data sources: Crossref
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Polyamines, ribonucleases, and the stability of RNA

Authors: T P, Karpetsky; P A, Hieter; J J, Frank; C C, Levy;

Polyamines, ribonucleases, and the stability of RNA

Abstract

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.

Related Organizations
Keywords

Ribonucleases, Bacteria, Drug Stability, Spermidine, Hydrolysis, Polynucleotides, Polyamines, RNA, Poly A

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selected citations
These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
39
Top 10%
Top 10%
Top 10%
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