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Mapping arm-DNA-binding domain interactions in AraC.

M Wu1, R Schleif

  • 1Biology Department, Johns Hopkins University, 3400 N. Charles St., Baltimore, MD, 21218, USA.

Journal of Molecular Biology
|April 5, 2001
PubMed
Summary
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Researchers identified mutations in the AraC protein

Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • The AraC protein regulates the l-arabinose operon in Escherichia coli.
  • It is proposed to function via a 'light switch' mechanism, requiring arabinose for activation.
  • Mutations affecting arm-DNA-binding domain interactions could lead to constitutive protein activity.

Purpose of the Study:

  • To identify mutations in the AraC DNA-binding domain that result in constitutive activity.
  • To investigate the role of specific residues in AraC protein function and regulation.

Main Methods:

  • Random mutagenesis of leucine residues in the AraC DNA-binding domain.
  • Systematic scanning of surface residues with alanine and glutamic acid.
  • Isolation and characterization of constitutive AraC mutants.

Related Experiment Videos

Main Results:

  • Identified 20 constitutive mutations at ten different positions within the AraC DNA-binding domain.
  • These mutations form a contiguous trail on the DNA-distal face.
  • The identified region likely represents the contact site between the N-terminal arm and the C-terminal DNA-binding domain.

Conclusions:

  • The study provides evidence for the 'light switch' mechanism of AraC regulation.
  • Specific residues in the DNA-binding domain are critical for regulating AraC's response to arabinose.
  • The findings elucidate the structural basis of AraC-mediated transcriptional activation.