Abstract
Optimal activity of chromatin-bound RNA polymerase from soybeans is obtained with 1 mm Mn2−, but only when high ionic strength or polyamines are included in the medium. Such inclusion does not increase the Mg2+ activation of the polymerase, but it does lower the concentration needed for optimum activity from 10 mm to 1 mm. Mg2− activation is inhibited by added Mn2+, and the inhibition is relieved by high ionic strength or spermidine. The RNA polymerase with either cation is almost entirely polymerase I at low and high ionic strength as evidenced by insensitivity to α-amanitin. Treatment of soybean seedlings with 2,4-dichlorophenoxyacetic acid does not change these characteristics; although the activity rises 3- to 4-fold.
It is suggested that chromatin as prepared here may be a selected fraction enriched in polymerase I, which is activated by either Mg2+ or Mn2+, and that the Mn2− inhibition of activity is due to a known reaction of Mn2− with DNA which can be relieved by high ionic strength.
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