The specific limited trypsinolysis of bacteriophage T7 RNA polymerase (T7RP) was performed in the presence of various components of the polymerase reaction and some GTP-analogs--irreversible inhibitors of the enzyme. The differences in the rate and sites of proteolysis were observed. Basing on the data obtained the role of the N-terminal domain of the T7RP in the interaction with promoter-containing template is proposed.
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