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Related Experiment Videos

2-5A-dependent RNase molecules dimerize during activation by 2-5A

B Dong1, R H Silverman

  • 1Department of Cancer Biology, Cleveland Clinic Foundation, Ohio 44195.

The Journal of Biological Chemistry
|February 24, 1995
PubMed
Summary
This summary is machine-generated.

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The enzyme 2-5A-dependent RNase becomes active when it forms homodimers. This activation requires binding to specific molecules called 2-5A oligoadenylates, forming the enzyme

Area of Science:

  • Molecular Biology
  • Enzymology
  • RNA Biology

Background:

  • 2-5A-dependent RNase is an interferon-inducible enzyme crucial for antiviral defense.
  • Its activity relies on binding to 2-5A oligoadenylates to degrade single-stranded RNA.

Purpose of the Study:

  • To investigate the quaternary structure of human 2-5A-dependent RNase.
  • To determine the role of 2-5A binding in enzyme activation and dimerization.

Main Methods:

  • Gel filtration chromatography
  • Chemical cross-linking
  • Glycerol gradient centrifugation
  • Monoclonal antibody production and use

Main Results:

  • Recombinant human 2-5A-dependent RNase forms stable homodimers upon binding to 2-5A.

Related Experiment Videos

  • Dimerization is dependent on the presence of functional 2-5A oligoadenylates.
  • The monomeric form is inactive, while the homodimeric form is catalytically active.

    • Conclusions:

    • The catalytically active form of 2-5A-dependent RNase is a homodimer.
    • 2-5A binding is essential for the transition from an inactive monomer to an active homodimer.