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Related Experiment Videos

Flipping a genetic switch by subunit exchange.

L J Lambert1, V Schirf, B Demeler

  • 1Laboratory of Molecular Biophysics, The Rockefeller University, 1230 York Avenue, Box 42, New York, NY 10021, USA.

The EMBO Journal
|December 18, 2001
PubMed
Summary
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The bacteriophage T4 AsiA protein acts as both a repressor and activator by modifying host RNA polymerase. Its structure reveals how dissociation of the AsiA homodimer alters gene expression and promoter selection.

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Microbiology

Background:

  • The bacteriophage T4 AsiA protein exhibits dual functionality, acting as both a repressor and activator of gene expression.
  • This regulation is achieved by altering the host RNA polymerase through interaction with sigma(70) conserved region 4 (SR4).

Purpose of the Study:

  • To elucidate the mechanism by which AsiA modulates gene expression.
  • To determine the three-dimensional structure of AsiA and its interaction with sigma(70) SR4.

Main Methods:

  • Three-dimensional structural analysis of the AsiA protein.
  • Elucidation of the interaction between AsiA and the sigma(70) SR4 domain.
  • Identification of protein interfaces involved in homodimer and heterodimer formation.

Related Experiment Videos

Main Results:

  • The structure of AsiA was determined to be a novel seven-helix bundle homodimer.
  • AsiA binds to sigma(70) SR4, altering RNA polymerase holoenzyme function.
  • Coincident protein interfaces necessitate dissociation of the AsiA homodimer to form an AsiA-SR4 heterodimer.

Conclusions:

  • The structural mechanism for AsiA's dual transcriptional role involves homodimer dissociation and heterodimer formation with sigma(70) SR4.
  • This subunit exchange mechanism underlies AsiA's ability to switch between repressor and activator functions, altering promoter selection by RNA polymerase.