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Related Experiment Videos

Engineering dimer-stabilizing mutations in the TATA-binding protein.

Haiping Kou1, B Franklin Pugh

  • 1Department of Biochemistry and Molecular Biology, The Pennsylvania State University, 452 N. Frear Laboratory, University Park, PA 16802, USA.

The Journal of Biological Chemistry
|March 17, 2004
PubMed
Summary
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TATA-binding protein (TBP) regulates gene transcription through dimerization. Stabilizing TBP dimers in vitro suppressed harmful cellular effects observed in vivo, confirming TBP

Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • TATA-binding protein (TBP) is crucial for eukaryotic transcription initiation.
  • TBP activity is regulated by dimerization, which can auto-inhibit DNA binding.
  • Disrupting TBP dimers in vitro causes decreased protein levels, transcriptional derepression, and growth toxicity in vivo.

Purpose of the Study:

  • To precisely define the in vivo multimeric structure of TBP.
  • To investigate the functional significance of TBP dimerization in vivo.
  • To validate the crystallographic dimer model of TBP.

Main Methods:

  • Site-directed mutagenesis based on the crystallographic dimer structure.
  • In vitro assays to assess TBP dimer stability.

Related Experiment Videos

  • In vivo studies to evaluate the effects of mutations on TBP phenotypes.

    • Main Results:

    • Mutations designed to enhance TBP dimer stability were successfully created.
    • Enhanced dimer stability in vitro correlated with suppressed in vivo phenotypes.
    • Intragenic suppression of dimer-destabilizing mutations provides strong evidence for TBP dimerization in vivo.

    Conclusions:

    • The crystallographic dimer configuration of TBP is relevant in vivo.
    • TBP dimerization is a critical regulatory mechanism for its function.
    • Stabilizing TBP dimers can mitigate negative cellular consequences.