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Updated: Jun 29, 2026

A Uniaxial Compression Experiment with CO2-Bearing Coal Using a Visualized and Constant-Volume Gas-Solid Coupling Test System
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Probing met repressor-operator recognition in solution.

Y Y He1, T McNally, I Manfield

  • 1Department of Genetics, University of Leeds, UK.

Nature
|October 1, 1992
PubMed
Summary
This summary is machine-generated.

The Escherichia coli methionine repressor (MetJ) uses beta-ribbon contacts for DNA recognition. Dimer-dimer interactions via alpha-helices are crucial for MetJ repression, confirming its DNA-protein interaction mechanism.

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Area of Science:

  • Structural biology
  • Molecular genetics
  • Biochemistry

Background:

  • The Escherichia coli methionine repressor (MetJ) regulates methionine biosynthesis genes.
  • Understanding DNA-protein interactions is key to gene regulation.
  • Previous models hypothesized MetJ-DNA binding mechanisms.

Purpose of the Study:

  • To investigate the role of specific structural features in MetJ-DNA binding.
  • To elucidate the mechanism of DNA sequence recognition by MetJ.
  • To assess the importance of dimer-dimer interactions in MetJ function.

Main Methods:

  • Three-dimensional crystal structure analysis of the MetJ-DNA complex.
  • Site-directed mutagenesis to disrupt protein-DNA and protein-protein contacts.
  • Assessment of repression efficiency in mutated MetJ proteins.

Main Results:

  • DNA sequence recognition is primarily mediated by hydrogen bonds between DNA bases and amino acid side chains in a beta-ribbon motif.
  • Antiparallel alpha-helices mediate dimer-dimer contacts between MetJ repressors bound to adjacent DNA sites.
  • Mutational analysis confirmed the beta-strand motif's role in recognition and highlighted the necessity of dimer-dimer interactions for effective repression.

Conclusions:

  • MetJ employs a beta-ribbon for direct DNA sequence recognition, a novel mode of interaction.
  • Dimer-dimer interactions mediated by alpha-helices are essential for MetJ's repressor function.
  • The carboxy-terminal helix face does not play a significant role in operator binding.