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Mediator subunit Med15 dictates the conserved “fuzzy” binding mechanism of yeast transcription activators Gal4 and Gcn4

Author

Listed:
  • Lisa M. Tuttle

    (Fred Hutchinson Cancer Research Center
    University of Washington)

  • Derek Pacheco

    (Fred Hutchinson Cancer Research Center
    Inventprise LLC)

  • Linda Warfield

    (Fred Hutchinson Cancer Research Center)

  • Damien B. Wilburn

    (University of Washington)

  • Steven Hahn

    (Fred Hutchinson Cancer Research Center)

  • Rachel E. Klevit

    (University of Washington)

Abstract

The acidic activation domain (AD) of yeast transcription factor Gal4 plays a dual role in transcription repression and activation through binding to Gal80 repressor and Mediator subunit Med15. The activation function of Gal4 arises from two hydrophobic regions within the 40-residue AD. We show by NMR that each AD region binds the Mediator subunit Med15 using a “fuzzy” protein interface. Remarkably, comparison of chemical shift perturbations shows that Gal4 and Gcn4, two intrinsically disordered ADs of different sequence, interact nearly identically with Med15. The finding that two ADs of different sequence use an identical fuzzy binding mechanism shows a common sequence-independent mechanism for AD-Mediator binding, similar to interactions within a hydrophobic cloud. In contrast, the same region of Gal4 AD interacts strongly with Gal80 via a distinct structured complex, implying that the structured binding partner of an intrinsically disordered protein dictates the type of protein–protein interaction.

Suggested Citation

  • Lisa M. Tuttle & Derek Pacheco & Linda Warfield & Damien B. Wilburn & Steven Hahn & Rachel E. Klevit, 2021. "Mediator subunit Med15 dictates the conserved “fuzzy” binding mechanism of yeast transcription activators Gal4 and Gcn4," Nature Communications, Nature, vol. 12(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-22441-4
    DOI: 10.1038/s41467-021-22441-4
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