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Related Experiment Videos

An RNA-binding chameleon.

C A Smith1, V Calabro, A D Frankel

  • 1Department of Biochemistry, University of California UCSF, San Francisco, CA 94143, USA.

Molecular Cell
|December 7, 2000
PubMed
Summary
This summary is machine-generated.

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The Jembrana disease virus Tat protein

Area of Science:

  • Structural biology
  • Virology
  • Molecular biology

Background:

  • Arginine-rich RNA binding motifs are common in viral regulatory proteins.
  • These domains can exhibit conformational flexibility and RNA-dependent folding.
  • Understanding protein-RNA interactions is crucial for viral regulation and pathogenesis.

Purpose of the Study:

  • To investigate the RNA binding properties and conformational adaptability of the Jembrana disease virus (JDV) Tat protein's RNA binding domain.
  • To explore the recognition of different target RNA structures, specifically TAR RNA from human immunodeficiency virus (HIV) and bovine immunodeficiency virus (BIV).
  • To elucidate the role of auxiliary proteins, like cyclin T1, in mediating high-affinity binding.

Main Methods:

  • Structural and biochemical analyses of the JDV Tat protein's RNA binding domain.

Related Experiment Videos

  • Comparative studies of binding to HIV TAR and BIV TAR RNA sequences.
  • Investigation of JDV Tat binding in the presence and absence of cyclin T1.

    • Main Results:

    • The JDV Tat RNA binding domain recognizes both HIV TAR and BIV TAR RNA sites.
    • The domain adopts distinct conformations and utilizes different amino acids for recognition depending on the bound RNA.
    • High-affinity binding to HIV TAR requires cyclin T1, while binding to BIV TAR does not.

    Conclusions:

    • The JDV Tat RNA binding domain exhibits "chameleon-like" conformational plasticity.
    • RNA structures can act as scaffolds, influencing protein folding and binding specificity.
    • This adaptability suggests mechanisms for evolving diverse RNA binding functions from a single domain.