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• W1966473729 abstract "The HIV transactivator, Tat, has been shown to be capable of potent repression of transcription initiation. Repression is mediated by the C-terminal segment of Tat, which binds the TFIID component, TAFII250, although the site(s) of interaction were not defined previously. We now report that the interaction between Tat and TAFII250 is extensive and involves multiple contacts between the Tat protein and TAFII250. The C-terminal domain of Tat, which is necessary for repression of transcription initiation, binds to a segment of TAFII250 that encompasses its acetyl transferase (AT) domain (885–1034 amino acids (aa)). Surprisingly, the N-terminal segment of Tat, which contains its activation domains, also binds to TAFII250 and interacts with two discontinuous segments of TAFII250 located between 885 and 984 aa and 1120 and 1279 aa. Binding of Tat to the 885–984 aa segment of TAFII250 requires the cysteine-rich domain of Tat, but not the acidic or glutamine-rich domains. Binding by the N-terminal domain of Tat to the 1120–1279 aa TAFII250 segment does not involve the acidic, cysteine- or glutamine-rich domains. Repression of transcription initiation by Tat requires functional TAFII250. We now demonstrate that transcription of the HIV LTR does not depend on TAFII250 which may account for its resistance to Tat mediated repression." @default.
• W1966473729 created "2016-06-24" @default.
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• W1966473729 date "2001-03-01" @default.
• W1966473729 modified "2023-10-14" @default.
• W1966473729 title "Extensive interactions between HIV TAT and TAFII250" @default.
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• W1966473729 doi "https://doi.org/10.1016/s0167-4838(01)00135-2" @default.
• W1966473729 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11257518" @default.
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