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Related Experiment Videos

Novel dimerization fold of RAP30/RAP74 in human TFIIF at 1.7 A resolution.

F Gaiser1, S Tan, T J Richmond

  • 1ETH Zürich, Institut fr Molekularbiologie und Biophysik, Zürich, Switzerland.

Journal of Molecular Biology
|February 24, 2001
PubMed
Summary

General transcription factor IIF (TFIIF), composed of RAP30 and RAP74, is crucial for RNA polymerase II transcription. Structural and mutation studies reveal its key interactions with DNA and other proteins for transcription initiation and elongation.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • General transcription factor IIF (TFIIF) is essential for transcription by RNA polymerase II.
  • TFIIF is a heterodimer of RNA polymerase-associated proteins RAP30 and RAP74.
  • TFIIF interacts with multiple components of the transcription machinery, including PolII, TFIIB, and TAF250.

Purpose of the Study:

  • To elucidate the structural basis of TFIIF function.
  • To understand the interactions of RAP30 and RAP74 with the transcription apparatus.
  • To investigate the role of specific structural features in transcription initiation and elongation.

Main Methods:

  • X-ray crystallography to determine the structure of RAP30/RAP74 interaction domains.
  • Mutagenesis studies to assess the functional importance of identified structural elements.

Related Experiment Videos

  • Biochemical assays to study protein-DNA and protein-protein interactions.

    • Main Results:

    • The X-ray structure revealed a novel "triple barrel" dimerization fold for the RAP30/RAP74 interaction domains.
    • Mutant data indicated that interactions with the transcription apparatus are mediated by the beta-barrel structure.
    • Flexible loops and other secondary structures extending from the core domain also contribute to interactions.

    Conclusions:

    • The tripartite beta-barrel fold is a key structural feature of TFIIF's interaction domains.
    • TFIIF utilizes both a stable core structure and flexible elements to engage with the transcription machinery.
    • These interactions are critical for the essential roles of TFIIF in transcription initiation and elongation.