Abstract
THE general transcripton factor TFIIE, together with other general transcription factors, is essential for transcription initiation by RNA polymerase II1–5. TFIIE stimulates the TFIIH-dependent kinase activity that phosphorylates the carboxy-terminal domain of the largest subunit of RNA polymerase II6, and possesses a helicase activity7. Here we show that human TFIIH has DNA-dependent ATPase activity and we characterize the stimulatory effect of TFIIE on both the ATPase and kinase activities. We demonstrate that extensive phosphorylation of RNA polymerase II occurs in a TFIIE-dependent manner in both the absence and presence of DNA but, in the latter case, only at a late stage of preinitiation complex assembly. We also show that TFIIH specifically phosphorylates three general transcription factors, human TFIIDτ (TBP), TFIIE-α and TFIIF-α (RAP74).
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Ohkuma, Y., Roeder, R. Regulation of TFIIH ATPase and kinase activities by TFIIE during active initiation complex formation. Nature 368, 160–163 (1994). https://doi.org/10.1038/368160a0
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DOI: https://doi.org/10.1038/368160a0
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