ACTIVATION OF PROKARYOTIC TRANSCRIPTION THROUGH ARBITRARY PROTEIN-PROTEIN CONTACTS

Many transcriptional activators in prokaryotes are known to bind near a promoter and contact RNA polymerase(1-5), but it is not dear whether a protein-protein contact between an activator and RNA polymerase is enough to activate gene transcription, Here we show that contact betwe en a DNA-bound protein and a heterologous protein domain fused to RNA polymerase can elicit transcriptional activation; moreover, the streng th of this engineered protein-protein interaction determines the amoun t of gene activation, Our results indicate that an arbitrary interacti on between a DNA-bound protein and RNA polymerase can activate transcr iption. We also find that when the DNA-bound 'activator' makes contact with two different components of the polymerase, the effect of these two interactions on transcription is synergistic.