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Related Experiment Videos

Herpes simplex virus type 1 polypeptide ICP4 bends DNA.

R D Everett1, J DiDonato, M Elliott

  • 1MRC Virology Unit, Glasgow, UK.

Nucleic Acids Research
|March 25, 1992
PubMed
Summary
This summary is machine-generated.

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Herpes simplex virus type 1's major regulatory protein, ICP4, bends DNA at its binding sites. This DNA bending by ICP4 and its DNA binding domain occurs near the ATCGTnnnnnCGG sequence, influencing viral gene activation.

Area of Science:

  • Molecular Biology
  • Virology
  • Structural Biology

Background:

  • ICP4 is the primary regulatory protein for herpes simplex virus type 1 (HSV-1).
  • ICP4 is crucial for activating transcription of most viral genes early in infection.
  • ICP4 functions as a DNA-binding protein recognizing specific sequences.

Purpose of the Study:

  • To investigate the structural impact of ICP4 binding on viral DNA.
  • To determine if ICP4 induces DNA bending at its recognition sites.
  • To characterize the DNA bending properties of both full-length ICP4 and its isolated DNA-binding domain.

Main Methods:

  • Purification of ICP4 protein from HSV-1 infected cells.
  • Isolation and purification of the DNA-binding domain of ICP4.

Related Experiment Videos

  • DNA electrophoretic mobility shift assays (EMSAs) to detect DNA binding.
  • Analysis of DNA bending induced by protein binding using gel electrophoresis.

    • Main Results:

    • Partially purified ICP4 induces a significant bend in DNA at its binding sites.
    • The isolated DNA-binding domain of ICP4 also bends DNA upon binding.
    • The DNA bending angles were similar at two distinct ICP4 binding sites.
    • The center of the DNA bend was located very close to the ICP4 binding sequence (ATCGTnnnnnCGG).

    Conclusions:

    • ICP4 binding to its cognate DNA sequences induces DNA bending.
    • The DNA-binding domain alone is sufficient to mediate this DNA bending.
    • This structural change in DNA may be important for the regulatory function of ICP4 in viral transcription.