Transcription of adenovirus 2 DNA by human RNA polymerase II in vitro.

The interaction of Adenovirus 2 DNA and human placental RNA polymerase II in vitro satisfies criteria that suggest that at least some fraction of our purified polymerase preparations corresponds to prokaryotic holoenzyme and is able to initiate transcription at "true" promoters: (1) The purified enzyme forms highly stable complexes at specific sites on Ad 2 DNA; Kass = 1--2 X 10(12) M-1. (2) Transcription of Ad 2 DNA from pre-formed complexes with human RNA polymerase II is resistant to poly I. (3) Many of the stable-binding sites correspond to Ad 2 promoters known to be active in vivo. We also present evidence consistent with a two-state (I and RS) model (Chamberlin et al. 1976; Travers 1974) for the interaction of human RNA polymerase II with Ad 2 DNA. These experiments, which are similar to those described previously in studies of wheat germ RNA polymerase II (Seidman et al. 1979), indicate that the mechanisms of transcription inhibition and promoter site selection in eukaryotic and prokaryotic systems may be very similar.