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The ς initiation factor ς 70  of  Escherichia coli  acts not only in promoter recognition and DNA strand opening, but also to mediate the transformation of RNA polymerase (RNAP) to an antiterminating form by the phage λ gene Q protein. Q is able to bind and modify RNAP when α 70 , still present in the initially elongating enzyme, recognizes a repeat of the −10 promoter element and induces a transcription pause. We have isolated mutations in the  rpoD  gene for ς 70  that impair Q function because they reduce the ability of ς 70  to recognize the downstream pause site. These mutations identify a locus of ς 70  that is important for the formation and stability of open promoter complex, likely because it mediates protein interactions with RNAP core.

A surface of Escherichia coli ς70 required for promoter function and antitermination by phage λ Q protein

A surface of Escherichia coli ς⁷⁰ required for promoter function and antitermination by phage λ Q protein