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The effect of spermine on transcription of mammalian chromatin by mammalian deoxyribonucleic acid-dependent ribonucleic acid polymerase
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Isolated rat liver nuclei demonstrate an increased ability to synthesize RNA in the presence of either spermine or spermidine. Spermidine has more effect on the low-salt α-amanitin-insensitive reaction, and spermine has more effect on the high-salt α-amanitin-sensitive reaction. Spermine is effective at concentrations of 0.1 mM and 1 muM, showing a biphasic effect. The RNA polymerase activity associated with nuclear chromatin is increased in the presence of spermine only at a concentration of 0.1 mM. Aso the transcription of deproteinized liver DNA by liver form-B polymerase or Escherichia coli enzyme is more efficient in the presence of 0.1 mM-spermine. Only when liver chromatin is transcribed by its homologous enzyme (and not by E. coli enzyme) is spermine active at both 0.1mM and 1 muM as in purified nuclei. The lower concentration of spermine (1 muM) is able to affect chromatin transcription by increasing the affinity of chromatin for the enzyme. Our findings suggest a regulatory role of spermine at the level of genome transcription.
Title: The effect of spermine on transcription of mammalian chromatin by mammalian deoxyribonucleic acid-dependent ribonucleic acid polymerase
Description:
Isolated rat liver nuclei demonstrate an increased ability to synthesize RNA in the presence of either spermine or spermidine.
Spermidine has more effect on the low-salt α-amanitin-insensitive reaction, and spermine has more effect on the high-salt α-amanitin-sensitive reaction.
Spermine is effective at concentrations of 0.
1 mM and 1 muM, showing a biphasic effect.
The RNA polymerase activity associated with nuclear chromatin is increased in the presence of spermine only at a concentration of 0.
1 mM.
Aso the transcription of deproteinized liver DNA by liver form-B polymerase or Escherichia coli enzyme is more efficient in the presence of 0.
1 mM-spermine.
Only when liver chromatin is transcribed by its homologous enzyme (and not by E.
coli enzyme) is spermine active at both 0.
1mM and 1 muM as in purified nuclei.
The lower concentration of spermine (1 muM) is able to affect chromatin transcription by increasing the affinity of chromatin for the enzyme.
Our findings suggest a regulatory role of spermine at the level of genome transcription.
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