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Dimerization of the operator binding domain of phage lambda repressor.

M A Weiss, C O Pabo, M Karplus

    Biochemistry
    |February 10, 1987
    PubMed
    Summary
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    Lambda repressor dimerization is crucial for DNA binding. Structural studies reveal how specific amino acid changes in the N-terminal domain disrupt this dimerization, impacting operator affinity.

    Area of Science:

    • Molecular Biology
    • Structural Biology
    • Biochemistry

    Background:

    • Dimerization of lambda repressor is essential for its ability to bind operator DNA.
    • Understanding the structural basis of this dimerization is key to comprehending DNA binding regulation.

    Purpose of the Study:

    • To investigate the dimerization properties of the N-terminal domain of lambda repressor.
    • To elucidate the structural basis for the coupling between dimer formation and operator binding.

    Main Methods:

    • Proton nuclear magnetic resonance (1H NMR) spectroscopy to monitor monomer-dimer equilibrium.
    • Gel filtration to assess protein size and quaternary structure.
    • Limited proteolysis to study the role of specific residues.

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    Main Results:

    • Wild-type and mutant N-terminal fragments of lambda repressor were analyzed.
    • 1H NMR confirmed conserved tertiary structure but revealed altered dimerization properties.
    • Specific mutations (Tyr-88----Cys, Ile-84----Ser) and residue removal (Val-91, Ser-92) disrupted dimer interface interactions.
    • Disruption of the dimer interface correlated with reduced operator binding affinity.

    Conclusions:

    • The dimer interface involves hydrophobic packing of helix 5 from symmetry-related monomers.
    • Specific amino acid substitutions and truncations significantly impair dimerization.
    • These structural changes explain the reduced operator binding affinity observed in mutant proteins.