. . . . . . . . . . . . . . . . . . . . . "HIV-1 Tat interacts with the RNA polymerase II holoenzyme complex that supports Tat-mediated transactivation of the HIV-1 LTR in vitro upon addition of TBP and TFIIB" . "Binding of HIV-1 Tat to TBP has been mapped to the cysteine rich and core domains (amino acids 20-50) of Tat and the H1 alpha helical and S2 domains (amino acids 163-220) of TBP" . "TBP interacts with HIV-1 Tat as part of the HIV-1 transcription preinitiation complex (PIC) and is necessary for Tat association with the PIC" . "TBP synergizes with HIV-1 Tat during Tat-mediated transactivation of the HIV-1 LTR promoter" . "HIV-1 Tat binds directly to the basal transcription factor TFIID through the TBP subunit of TFIID" . "Interaction of TBP/TFIID with the HIV-1 LTR, and therefore presumably HIV-1 Tat, is primarily dependent on the LTR TATA element and may also be stabilized or regulated by flanking E box motifs and basic helix-loop-helix proteins such as AP-4 and E47" . "Inhibition of HIV-1 Tat by p53 is mediated through the Sp1 and TATA box of the HIV-1 LTR, suggesting p53 interferes with the interaction between Tat and TBP during LTR transactivation" . "TBP is required for HIV-1 Tat-mediated transactivation of the HIV-1 LTR promoter" . "Binding of HIV-1 Tat to the TBP subunit of TFIID stabilizes the interaction of TFIID with TFIIA" . "HIV-1 Tat competes for Dr1 interaction with TBP" . "Recruitment of TBP to the HIV-1 LTR promoter is a limiting step for HIV-1 Tat transactivation, however interaction of Tat with TBP/TFIID occurs after this recruitment" . "HIV-1 Tat directly interacts with TBP as demonstrated by Tat-affinity column purification" . "Binding of HIV-1 Tat to p300 induces a conformational change in the CBP/p300 complex such that it can acquire and bind better to basal transcription factors such as TBP, indicating Tat helps CBP/p300 recruit new partners to the transcription machinery" . "interacts with" . "requires" . "binds" . "recruits" . "stabilizes" . "synergizes with" . .