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Related Experiment Videos

Dimerization of the TATA binding protein

R A Coleman1, A K Taggart, L R Benjamin

  • 1Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park 16802, USA.

The Journal of Biological Chemistry
|June 9, 1995
PubMed
Summary
This summary is machine-generated.

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The TATA binding protein (TBP) dimerizes in its inactive state. This dimerization must be reversed for TBP to bind DNA, potentially slowing down transcription complex assembly.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • TATA binding protein (TBP) is essential for eukaryotic transcription.
  • TBP recruitment to promoters is a slow, potentially rate-limiting step in transcription complex assembly.

Purpose of the Study:

  • Investigate the physical state of TBP before DNA binding.
  • Understand the nature of the rate-limiting step in TBP recruitment.

Main Methods:

  • Chemical cross-linking
  • Gel filtration chromatography
  • Protein affinity chromatography

Main Results:

  • Human TBP's DNA binding domain dimerizes when not bound to DNA.
  • TBP dimers are stable (low nanomolar KD) and primarily interact via hydrophobic forces.

Related Experiment Videos

  • TBP dimers do not bind DNA; they must dissociate into monomers first.

    • Conclusions:

    • The slow dissociation of stable TBP dimers may limit the kinetics of TBP's DNA binding.
    • This finding supports the dimeric structure of TBP observed in other species.
    • The dimerization state of TBP is a critical factor in regulating transcription initiation.