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Related Experiment Videos

Yeast transcript elongation factor (TFIIS), structure and function. II: RNA polymerase binding, transcript cleavage,

D E Awrey1, N Shimasaki, C Koth

  • 1C.H. Best Institute, Banting and Best Department of Medical Research, University of Toronto, Toronto, Ontario M5G 1L6, Canada.

The Journal of Biological Chemistry
|August 26, 1998
PubMed
Summary

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This summary is machine-generated.

The yeast transcription factor TFIIS

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • TFIIS is a crucial transcription elongation factor for RNA polymerase II.
  • The active fragment of TFIIS includes a helix bundle, zinc ribbon, and linker.
  • Understanding TFIIS function requires detailed structural and functional analysis.

Purpose of the Study:

  • To investigate the functional roles of TFIIS domains using structure-guided mutagenesis.
  • To elucidate the mechanism by which TFIIS promotes transcription elongation and transcript cleavage.
  • To identify key residues and regions involved in RNA polymerase II binding and TFIIS activity.

Main Methods:

  • Structure-guided mutagenesis of the TFIIS transcription elongation factor.
  • Assays to measure RNA polymerase II binding affinity.

Related Experiment Videos

  • In vitro transcription assays to assess transcript cleavage and read-through activity.

    • Main Results:

    • The helix bundle domain binds RNA polymerase II with high affinity, mediated by a basic patch.
    • Mutations disrupting polymerase binding abolish TFIIS transcription activity.
    • Mutations in the zinc ribbon and linker regions impair transcript cleavage and read-through.
    • Specific aromatic residues (Phe269, Phe296, Phe308) in the zinc ribbon are critical for function.
    • Linker region mutations (residues 240-245, 250-255) also severely impact TFIIS activity.

    Conclusions:

    • RNA polymerase II binding is essential for TFIIS function in transcription elongation.
    • The zinc ribbon and linker regions are critical for TFIIS-mediated transcript cleavage and read-through.
    • The TFIIS linker region likely adopts a specific structure within the elongation complex to facilitate its function.