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trp repressor mutations alter DNA complex stoichiometry

Y C Liu1, K S Matthews

  • 1Department of Biochemistry and Cell Biology, Rice University, Houston, Texas 77251-1892.

The Journal of Biological Chemistry
|January 21, 1994
PubMed
Summary
This summary is machine-generated.

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Mutant trp repressors exhibit altered DNA binding stoichiometry and affinity compared to wild-type, influenced by operator sequence and corepressor. These findings reveal complex interactions within the repressor-operator system.

Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • The trp repressor regulates gene expression by binding to operator DNA sequences.
  • Mutations in the trp repressor can alter its DNA binding properties and regulatory function.
  • Understanding these interactions is crucial for elucidating gene regulation mechanisms.

Purpose of the Study:

  • To investigate the DNA binding behavior of mutant trp repressors using gel retardation assays.
  • To characterize the stoichiometry and affinity of protein-DNA complexes formed by wild-type and mutant repressors.
  • To determine the influence of operator sequence, corepressor, and protein structure on trp repressor binding.

Main Methods:

  • Gel retardation assays were employed to study the interaction of trp repressor mutants with various operator DNA sequences.

Related Experiment Videos

  • Analysis of protein-DNA complex stoichiometry and binding patterns.
  • Investigation of binding under different conditions, including varying operator sequences and corepressors.

    • Main Results:

    • Superrepressor mutants (EK13, EK18, EK49) formed higher stoichiometry complexes (three dimers/operator) with TrpEDCBA operator compared to wild-type (two dimers/operator).
    • Mutant DN46 showed a more prominent single dimer-operator complex, despite higher apparent affinity.
    • The formation of higher-order complexes was dependent on the presence of two operator half-sites and could be influenced by ligands like 5-methyl-tryptophan.

    Conclusions:

    • Trp repressor DNA binding is a complex process influenced by operator sequence, corepressor identity, and intra/inter-dimeric interactions.
    • Mutations can significantly alter binding stoichiometry and affinity, impacting gene regulation.
    • The N-terminal regions of the trp repressor likely play a role in these interactions.