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Related Experiment Videos

Self-assembly properties of a model RING domain.

Alex Kentsis1, Ronald E Gordon, Katherine L B Borden

  • 1Department of Physiology and Biophysics, Mount Sinai School of Medicine, New York University, New York, NY 10029, USA.

Proceedings of the National Academy of Sciences of the United States of America
|January 17, 2002
PubMed
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Arenaviral protein Z

Area of Science:

  • Structural biology
  • Virology
  • Biochemistry

Background:

  • RING domains are crucial for cellular processes but lack a defined general function.
  • Arenaviral protein Z, primarily composed of a RING domain, forms spherical structures in infected cells.

Purpose of the Study:

  • To elucidate the thermodynamic and kinetic mechanisms underlying RING domain-dependent self-assembly.
  • To explore the potential general function of RING domains in forming macromolecular scaffolds.

Main Methods:

  • In vitro self-assembly assays of purified arenaviral protein Z.
  • Biophysical techniques to analyze assembly thermodynamics and kinetics.
  • Investigation of conformational changes and zinc coordination within the RING domain.

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Main Results:

  • Purified arenaviral protein Z self-assembles into spherical structures in vitro.
  • Assembly is thermodynamically and kinetically characterized, revealing a coupled conformational reorganization.
  • Changes in zinc coordination at site II of the RING domain are observed during assembly.

Conclusions:

  • The self-assembly of arenaviral protein Z provides a model for RING domain-mediated scaffold formation.
  • Conformational reorganization can be rate-limiting in macromolecular scaffold assembly, similar to protein folding.
  • RING domains may have a general role in constructing macromolecular scaffolds for integrating cellular biochemical processes.