After TFIID, TFIIA, TFIIB recruit Pol II, TFIIE is recruited and in turn, recruits TFIIH. TFIIE is positioned as a molecular latch, locking down TFIIH and limiting overall TFIIH flexibility. The XPB translocase will negatively supercoil the initiator element (INR) DNA to open it for Pol II. Pol II C-terminal domain (CTD) phosphorylation by the CAK kinase module in the ten-subunit TFIIH will promote Pol II release from the INR.