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The lambda repressor contains two domains.

C O Pabo, R T Sauer, J M Sturtevant

    Proceedings of the National Academy of Sciences of the United States of America
    |April 1, 1979
    PubMed
    Summary
    This summary is machine-generated.

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    Lambda phage repressor comprises two domains linked by a protease-sensitive connector. The N-terminal domain binds DNA, while the C-terminal domain facilitates oligomerization, as shown by protease digestion and calorimetry.

    Area of Science:

    • Molecular Biology
    • Protein Structure and Function

    Background:

    • The lambda phage repressor protein regulates viral gene expression.
    • Understanding its domain structure is crucial for deciphering its regulatory mechanisms.

    Purpose of the Study:

    • To elucidate the domain organization and functional properties of the lambda phage repressor.
    • To identify the structural elements responsible for DNA binding and oligomerization.

    Main Methods:

    • Proteolytic digestion using papain to generate protein fragments.
    • Differential scanning calorimetry to assess protein thermal stability and denaturation profiles.

    Main Results:

    • Papain digestion yielded two stable fragments: an N-terminal (residues 1-92) and a C-terminal (residues 132-236) domain.

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  • Calorimetry revealed distinct denaturation temperatures for each fragment (50°C and 70°C, respectively).
  • Intact repressor exhibited two denaturation transitions, mirroring the fragment denaturation profiles.

    • Conclusions:

    • Lambda phage repressor is composed of two distinct domains connected by a protease-sensitive linker region.
    • The N-terminal domain is responsible for DNA binding.
    • The C-terminal domain mediates protein oligomerization.