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Operator binding by lambda repressor heterodimers with one or two N-terminal arms

Y I Kim1, J C Hu

  • 1Department of Biochemistry and Biophysics, Texas A&M University, College Station 77843-2128, USA.

Proceedings of the National Academy of Sciences of the United States of America
|August 1, 1995
PubMed
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Both flexible arms of the bacteriophage lambda cI repressor are essential for optimal operator DNA binding and discrimination. Even though one arm appears sufficient, the study demonstrates the necessity of both for normal function.

Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Bacteriophage lambda cI repressor is crucial for regulating viral gene expression.
  • The repressor protein functions as a dimer, with each monomer possessing a DNA-binding domain and a flexible N-terminal arm.
  • The N-terminal arm (Ser1-Thr2-Lys3-Lys4-Lys5-Pro6) is known to interact with operator DNA.

Purpose of the Study:

  • To investigate the functional necessity of the two N-terminal arms of the lambda cI repressor in operator DNA binding.
  • To determine if one arm is sufficient for DNA binding or if both are required for optimal function and specificity.

Main Methods:

  • Construction of heterodimeric lambda repressors with varying numbers of functional arms (two, one, or zero).
  • Fusion of the lambda repressor DNA-binding domain with leucine zippers from Fos and Jun to create heterodimers.

Related Experiment Videos

  • Assessment of operator binding affinity and site discrimination capabilities of the engineered repressor variants.

    • Main Results:

    • Heterodimeric repressors lacking one or both N-terminal arms exhibited reduced operator binding affinity.
    • Site discrimination was significantly impaired in repressors with only one or no functional arm.
    • Despite crystallographic evidence showing only one arm in the N-domain-operator complex, functional assays confirmed the requirement of both arms.

    Conclusions:

    • Both N-terminal arms of the bacteriophage lambda cI repressor are essential for high-affinity operator binding.
    • The presence of both arms is critical for the repressor's ability to discriminate between different operator sites.
    • These findings highlight the cooperative role of both arms in the precise regulation of bacteriophage lambda gene expression.