Abstract
SummaryYeast RNA polymerase (Pol) II general factor TFIIE and the TFIIH subunit Ssl2/XPB function in transition of the preinitiation complex (PIC) to the open complex. We find that the three TFIIE winged helix (WH) domains form a heterodimer, with the Tfa1/TFIIEα WH binding the Pol II clamp and the Tfa2/TFIIEβ tandem WH domain encircling promoter DNA that becomes single stranded in the open complex. Ssl2 lies adjacent to TFIIE, enclosing downstream promoter DNA. In contrast to previous proposals, comparison of the PIC and open complex models strongly suggests that Ssl2 promotes DNA opening by functioning as a double stranded DNA translocase, feeding 15 bp of double stranded DNA into the Pol II cleft. Right-handed threading of DNA through the Ssl2 binding groove, combined with the fixed position of upstream promoter DNA, will lead to DNA unwinding and the open state.
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