Nucleotide-Dependent Inactivation of RNA Polymerase from Bacillus brevis

AUTOR(ES)
RESUMO

RNA polymerase has been purified from vegetative cells of Bacillus brevis and resolved into “core” enzyme and sigma factor. The purified enzyme is rapidly inactivated by incubation at low temperatures in the presence of 1-2 mM ATP, dATP, or NAD+, while other nucleotides at this concentration have little or no effect. Inactivation is not accompanied by the incorporation of an adenylyl or phosphoryl moiety into RNA polymerase; nevertheless, it is essentially irreversible. DNA, high concentrations of glycerol, as well as low concentrations (1 mM) of orthophosphate protect RNA polymerase from the nucleotide-dependent inactivation.

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