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P22 c2 repressor. Domain structure and function.

J De Anda, A R Poteete, R T Sauer

    The Journal of Biological Chemistry
    |September 10, 1983
    PubMed
    Summary
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    The bacteriophage P22 c2 repressor protein has two distinct functional domains. The NH2-terminal domain binds DNA and controls transcription, while the COOH-terminal domain influences protein structure.

    Area of Science:

    • Molecular biology
    • Bacteriophage genetics
    • Protein structure-function relationships

    Background:

    • The c2 repressor protein is crucial for regulating gene expression in bacteriophage P22.
    • Understanding repressor protein domains is key to deciphering viral genetic control mechanisms.

    Purpose of the Study:

    • To investigate the functional and structural domains of the bacteriophage P22 c2 repressor.
    • To determine the specific roles of the NH2-terminal and COOH-terminal regions in DNA binding and transcriptional regulation.

    Main Methods:

    • Proteolytic digestion of the c2 repressor using enzymes like trypsin, chymotrypsin, and elastase.
    • Purification and characterization of resulting NH2-terminal and COOH-terminal protein fragments.
    • Analysis of DNA-binding affinity to P22 operator sequences.

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  • Assessment of transcriptional control (positive and negative) mediated by the fragments.
  • Investigation of protein oligomerization properties of the fragments.

    • Main Results:

    • The c2 repressor can be cleaved into stable NH2-terminal and COOH-terminal fragments.
    • NH2-terminal fragments retain specific DNA-binding capacity and transcriptional regulatory functions.
    • COOH-terminal fragments do not bind DNA but exhibit concentration-dependent oligomerization.
    • These findings indicate a modular structure for the c2 repressor.

    Conclusions:

    • The bacteriophage P22 c2 repressor possesses at least two distinct structural and functional domains.
    • The NH2-terminal domain is responsible for DNA binding and transcriptional regulation.
    • The COOH-terminal domain mediates protein oligomerization, a process important for repressor function.
    • This domain organization is analogous to that observed in the related lambda phage cI repressor.