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Repressor of phage 16-3 with altered binding specificity indicates spatial differences in repressor-operator

Szilamér Ferenczi1, László Orosz, Péter P Papp

  • 1Institute of Genetics, Agricultural Biotechnology Center, Gödöllõ, Szent-Györgyi A. 4., H-2100, Hungary.

Journal of Bacteriology
|February 3, 2006
PubMed
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Researchers identified a mutant C repressor protein that alters DNA binding specificity. This finding reveals spatial differences in how the repressor interacts with different DNA operator sequences, impacting phage lysogeny.

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Virology

Background:

  • The C repressor protein of phage 16-3 is crucial for establishing and maintaining lysogeny.
  • This repressor recognizes distinct DNA operator sequences differing in spacer length.
  • A model of rotationally flexible protein homodimers has been proposed to explain repressor adaptability.

Purpose of the Study:

  • To isolate a repressor mutant with altered DNA binding specificity.
  • To identify specific residue-base pair contacts.
  • To investigate the spatial relationship between the repressor and DNA in different operator complexes.

Main Methods:

  • Isolation and characterization of a mutant C repressor protein.
  • Analysis of repressor-operator complex structures.

Related Experiment Videos

  • Monitoring spatial interactions within the major groove of DNA.

    • Main Results:

    • A repressor mutant with altered binding specificity was successfully isolated.
    • A specific residue-base pair contact was identified.
    • Spatial differences at the repressor-DNA interface were observed, suggesting varied docking arrangements.

    Conclusions:

    • The C repressor exhibits conformational flexibility in recognizing structurally different operators.
    • Mutant analysis provides insights into the molecular mechanisms of repressor-operator recognition.
    • Findings contribute to understanding the regulation of phage lysogeny.