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Nature, Vol.386, No.6625, 627-630, 1997
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 between a DNA-bound protein and a heterologous protein domain fused to RNA polymerase can elicit transcriptional activation; moreover, the strength of this engineered protein-protein interaction determines the amount of gene activation, Our results indicate that an arbitrary interaction between a DNA-bound protein and RNA polymerase can activate transcription. 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.
Keywords:RNA-POLYMERASE-II;CAMP RECEPTOR PROTEIN;ESCHERICHIA-COLI;LAMBDA-REPRESSOR;SYNERGISTIC ACTIVATION;GENE ACTIVATION;ALPHA-SUBUNIT;PROMOTER;RECOGNITION;INITIATION