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Related Experiment Videos

Srb/mediator proteins interact functionally and physically with transcriptional repressor Sfl1

W Song1, M Carlson

  • 1Departments of Genetics and Development, Columbia University, 701 W. 168th St., New York, NY 10032, USA.

The EMBO Journal
|October 2, 1998
PubMed
Summary

Saccharomyces cerevisiae Sfl1 protein interacts with Srb/mediator proteins to repress transcription. This interaction involves Sfl1 binding DNA and inhibiting RNA polymerase II holoenzyme activity, crucial for gene regulation.

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Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Mediator (Srb/Mediator) proteins are crucial for RNA polymerase II holoenzyme function.
  • These proteins are implicated in transcriptional repression in Saccharomyces cerevisiae.
  • The SFL1 gene's role in this process was not fully understood.

Purpose of the Study:

  • To investigate the functional relationship between SFL1 and Srb/Mediator proteins in transcriptional repression.
  • To elucidate the mechanism by which Sfl1 mediates repression.
  • To determine if Sfl1 directly interacts with Mediator components.

Main Methods:

  • Genetic analysis of SUC2 repression defects and SFL1 dosage.
  • In vitro DNA binding assays for Sfl1.

Related Experiment Videos

  • Reporter gene assays using LexA-Sfl1 fusion protein.
  • Co-immunoprecipitation experiments to detect protein interactions.

    • Main Results:

    • Mutations in SRB8, SRB9, SRB11, SIN4, or ROX3, affecting Mediator function, were suppressed by increased SFL1 dosage.
    • Sfl1 binds to a repression site upstream of the SUC2 TATA box.
    • LexA-Sfl1 fusion protein repressed transcription, with reduced repression in an srb9 mutant.
    • Sfl1 co-immunoprecipitated with Srb9, Srb11, Sin4, and Rox3.

    Conclusions:

    • Sfl1 functions in transcriptional repression in Saccharomyces cerevisiae.
    • Sfl1 interacts with specific Srb/Mediator proteins (Srb9, Srb11, Sin4, Rox3).
    • Sfl1 likely inhibits RNA polymerase II holoenzyme activity by interacting with Mediator proteins bound to DNA.