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  • Solution Structure Of A Tbp-taf(ii)230 Complex: Protein Mimicry Of The Minor Groove Surface Of The Tata Box Unwound By Tbp
  • Engineering
  • Environmental Engineering
  • Air Pollution Modelling And Control
  • Solution Structure Of A Tbp-taf(ii)230 Complex: Protein Mimicry Of The Minor Groove Surface Of The Tata Box Unwound By Tbp

    • Related Experiment Videos

    Solution structure of a TBP-TAF(II)230 complex: protein mimicry of the minor groove surface of the TATA box unwound by TBP

    D Liu1, R Ishima, K I Tong

    • 1Department of Medical Biophysics, University of Toronto, Ontario, Canada.

    Cell
    |September 19, 1998

    View abstract on PubMed

    Summary
    This summary is machine-generated.

    The N-terminal region of Drosophila TAF(II)230 binds TBP, inhibiting transcription. Its structure mimics the TATA box, explaining how TAF(II)230 regulates TFIID activity.

    Related Experiment Videos

    Area of Science:

    • Molecular Biology
    • Structural Biology
    • Biochemistry

    Background:

    • General transcription factor TFIID is crucial for regulating gene transcription.
    • TFIID comprises TATA box-binding protein (TBP) and TBP-associated factors (TAFs).
    • The Drosophila TAF(II)230 (dTAF(II)230) N-terminal region inhibits TBP's DNA binding.

    Purpose of the Study:

    • To determine the solution structure of the complex between the dTAF(II)230 N-terminal region and TBP.
    • To elucidate the structural mechanism by which dTAF(II)230 inhibits TBP binding to the TATA box.

    Main Methods:

    • Nuclear Magnetic Resonance (NMR) spectroscopy to determine the solution structure.
    • Analysis of protein-protein interactions within the TFIID complex.

    Main Results:

    • The N-terminal region of dTAF(II)230 (residues 11-77) forms a stable complex with TBP.
    • The dTAF(II)230(11-77) structure consists of three alpha helices and a beta hairpin.
    • This structure occupies the DNA-binding surface of TBP, mimicking the TATA box minor groove.
    • This mimicry explains the inhibitory effect of dTAF(II)230 on TBP-TATA box interaction.

    Conclusions:

    • The structural mimicry of the TATA element by dTAF(II)230 provides a molecular basis for negative transcriptional regulation.
    • This finding offers insights into the intricate mechanisms of transcription factor assembly and function.
    • Understanding these interactions is key to deciphering gene expression control.