Abstract
Mustine inhibits the template activity of chromatin and DNA in an RNA-polymerase system in vitro much more strongly than its monofunctional analogue. Chromatin is more sensitive to the action of mustine than is deproteinized DNA. However, the template activity of DNA is reduced to a greater degree by the action of the monofunctional analogue of mustine than is that of chromatin. The mechanism of inhibition of the template activity of chromatin by mustine is probably connected with the ability of the compound to form DNA-protein cross-linkages in the chromatin structure.
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