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Related Experiment Videos

A collapsed state functions to self-chaperone RNA folding into a native ribonucleoprotein complex.

A E Webb1, K M Weeks

  • 1Department of Chemistry, University of North Carolina, Chapel Hill, North Carolina 27599-3290, USA.

Nature Structural Biology
|February 15, 2001
PubMed
Summary

Large RNAs like bI5 intron RNA use collapsed states to self-chaperone folding, preventing premature protein cofactor binding. This mechanism ensures proper assembly of complex RNA-protein machines.

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Protein-dependent transition states for ribonucleoprotein assembly.

Journal of molecular biology·2001

Area of Science:

  • Structural Biology
  • Molecular Biology
  • RNA Folding

Background:

  • Large RNAs require protein cofactors for their active, native structures.
  • The bI5 group I intron RNA exists in multiple conformational states (expanded, collapsed, native) influenced by Mg(2+) concentration.

Purpose of the Study:

  • To investigate the role of RNA conformational states in protein cofactor interaction and folding.
  • To understand the self-chaperoning mechanism of bI5 RNA folding.

Main Methods:

  • Manipulation of RNA states using varying Mg(2+) concentrations.
  • Hydroxyl radical footprinting to map RNA-protein interactions.
  • Functional splicing experiments to assess complex productivity.

Main Results:

Related Experiment Videos

  • bI5 RNA rapidly folds into a non-native collapsed state under near-physiological conditions.
  • The CBP2 protein cofactor facilitates the transition from the collapsed to the native state.
  • CBP2 binding to the expanded RNA state leads to non-native interactions and kinetically trapped complexes.

Conclusions:

  • The collapsed state acts as a self-chaperone, preventing premature CBP2 binding and ensuring proper RNA folding.
  • This self-chaperoning mechanism is crucial for preventing misassembly of large RNA-protein complexes in cells.