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Related Experiment Videos

DNA structural variations in the E. coli tyrT promoter.

H R Drew, A A Travers

    Cell
    |June 1, 1984
    PubMed
    Summary
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    DNA structure varies with base sequence, influencing protein recognition. Three nucleases reveal DNA backbone geometry, not just sequence, dictates cleavage patterns, highlighting structural polymorphism.

    Area of Science:

    • Molecular Biology
    • Structural Biology
    • Biochemistry

    Background:

    • DNA structure is a double helix sensitive to base sequence.
    • Base sequence variations induce structural deformations in the DNA backbone.
    • Proteins and DNA-binding reagents recognize these structural changes.

    Purpose of the Study:

    • To investigate the interactions of common nucleases with a natural DNA sequence.
    • To determine if nucleases are sensitive to DNA base sequence or backbone geometry.
    • To provide evidence for DNA structural polymorphism.

    Main Methods:

    • Analysis of DNA cleavage patterns using three nucleases: DNAase I, DNAase II, and copper-phenanthroline.
    • Examination of a 160 bp tyrT promoter DNA sequence at single-bond resolution.

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  • Correlation of cleavage sites with DNA structural features.

    • Main Results:

    • All three nucleases exhibited sensitivity to DNA backbone geometry rather than base sequence.
    • Sequence-dependent cleavage patterns indicated structural polymorphism in DNA.
    • Observed variations included helix groove width, radial asymmetry, and phosphate accessibility.

    Conclusions:

    • DNA structural polymorphism influences the recognition of DNA by binding reagents.
    • Base composition and purine-pyrimidine asymmetry affect DNA recognition through structural changes.
    • Understanding DNA geometry is crucial for explaining sequence-specific interactions.