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The structure of intrinsically disordered activation domains (ADs) influences gene expression. Changes in the ensemble dimensions of the HIF-1α activation domain altered its transcriptional activity, revealing a sequence-dependent link.

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Transcription factors regulate gene transcription by binding to DNA promoter sequences.
  • Eukaryotic transcription factors often possess intrinsically disordered activation domains (ADs) that modulate their activity.
  • Disordered protein regions, including ADs, lack fixed structures and exist as conformational ensembles with sequence-encoded preferences.

Purpose of the Study:

  • To investigate the relationship between the structural preferences of disordered activation domain ensembles and their ability to induce gene expression.
  • To test the hypothesis that the conformational ensemble dimensions of ADs are linked to their transcriptional function.

Main Methods:

  • Utilized Förster Resonance Energy Transfer (FRET) microscopy to measure the ensemble dimensions of activation domains in live cells.
  • Introduced point mutations into activation domains to alter their ensemble dimensions.
  • Correlated measured structural changes with changes in transcriptional activity.

Main Results:

  • Point mutations that expanded the ensemble of the HIF-1α activation domain increased its transcriptional activity.
  • Mutations that compacted the HIF-1α ensemble reduced its transcriptional activity.
  • The CITED2 activation domain showed no correlation between ensemble dimensions and transcriptional activity.

Conclusions:

  • A sequence-dependent relationship exists between the ensemble dimensions of intrinsically disordered activation domains and their transcriptional activity.
  • The structural dynamics of ADs play a critical role in regulating gene expression.
  • Findings highlight the functional significance of conformational flexibility in disordered protein regions.