RNA polymerase activity and template activity of chromatin after butyrate induced hyperacetylation of histones in Physarum.

We have studied the effect of sodium-n-butyrate on endogenous RNA polymerase in Physarum polycephalum. 1 mM butyrate strongly reduces RNA polymerase activity measured in isolated nuclei or chromatin; both RNA polymerase A as well as the alpha-amanitin sensitive RNA polymerase B are equally affected. Despite a concomitant hyperacetylation of histone H4 the template activity of chromatin, as analyzed by in vitro transcription of the chromatin with exogenous RNA polymerase from E. coli or RNA polymerase II from wheat germ, remains unaltered as compared to untreated control chromatin, indicating that there is no positive correlation between histone acetylation and template activity of chromatin for transcription in this organism. The results further indicate, that butyrate acts primarily as a quick but reversible inhibitor of protein synthesis in Physarum; the fast decrease of endogenous RNA polymerase activity after butyrate treatment is due to inhibition of enzyme synthesis rather than inactivation of other factors necessary for transcription.