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Primary structure of the lambda repressor.

R T Sauer, R Anderegg

    Biochemistry
    |March 21, 1978
    PubMed
    Summary
    This summary is machine-generated.

    Researchers determined the complete covalent structure of the bacteriophage lambda repressor, a protein with 236 amino acids. This acidic protein features a polar, basic amino-terminal region with clustered lysines and arginines.

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    Area of Science:

    • Molecular Biology
    • Protein Chemistry
    • Genetics

    Background:

    • Bacteriophage lambda repressor (cI) is crucial for lysogenic cycle.
    • Understanding its structure is key to its function.

    Purpose of the Study:

    • To elucidate the complete covalent structure of the bacteriophage lambda repressor protein.

    Main Methods:

    • Sequential Edman degradation for amino acid sequencing.
    • Gas chromatographic-mass spectrometric peptide sequencing.
    • DNA sequencing of the repressor gene (cI).

    Main Results:

    • The bacteriophage lambda repressor is a single-chain protein.
    • It comprises 236 amino acids and is acidic in nature.

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  • The N-terminal 40 residues are highly polar and basic, with clustered lysines and arginines.

    • Conclusions:

    • The determined covalent structure provides a foundation for understanding repressor function.
    • This structural information is vital for phage-genetics research.