Abstract
The synthesis of RNA catalysed by RNA polymerase from Escherichia coli is terminated at specific sites on DNA templates through the action of a multimeric basic protein known as rho (refs 1, 2). Three lines of evidence suggest that an interactions of rho with the nascent RNA is important for this termination. First, rho binds strongly to RNA; second, rho expresses an RNA-dependent ATPase activity which is essential for termination; third, RNA polymerase does not terminate RNA synthesis at rho-dependent sites when the nascent RNA is digested by ribonuclease during transcription. From the fact that certain RNAs, particularly single-stranded, pyrimidine-rich polymers containing at least 10% cytidylate residues, are more effective than other RNAs at promoting rho-ATPase, it has been proposed that rho recognises specific sites oion on a mRNA transcribed from bacteriophage lambda DNA.
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