Abstract
Highly purified rho termination factor from Escherichia coli catalyzes an RNA-dependent hydrolysis of ribonucleoside triphosphates to nucleoside diphosphates and inorganic phosphate. In the presence of poly(C), a specific activity of 100 μmole of ATP hydrolyzed per min/mg has been measured. The phosphohydrolase activity appears to be associated with the protein responsible for termination of RNA synthesis, but a functional relationship between the two activities is not yet evident. Hydrolysis of nucleoside triphosphates occurs in the absence of termination and without any extensive degradation of RNA.
Keywords: Escherichia coli, RNA polymerase, transcription
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Selected References
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