Abstract
We have purified two general transcription factors (FA and FE) necessary for specific transcription by mammalian RNA polymerase II to near homogeneity. Both activities are associated with peptides of approximately 33 kDa. FA and FE do not replace one another and show different kinetics of action in a sarkosyl block assay. In particular, FE participated in a rapid reaction after the formation of an initial complex with the other transcription factors. Furthermore, FE can associate with purified calf thymus RNA polymerase II.
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