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A collapsed non-native RNA folding state.

K L Buchmueller¹, A E Webb, D A Richardson

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

Nature Structural Biology

|May 10, 2000

Summary

This summary is machine-generated.

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The bI5 group I intron RNA collapses into a non-native state at low magnesium concentrations, distinct from typical kinetic traps. This collapsed state may precede the assembly of other ribonucleoprotein complexes.

Area of Science:

Biochemistry
Molecular Biology
RNA Structure

Background:

Group I introns are ribozymes with complex folding pathways.
RNA structure is highly dependent on ion concentrations, particularly Mg2+.
Understanding RNA folding is crucial for understanding biological function.

Purpose of the Study:

To investigate the folding pathway of the bI5 group I intron RNA at physiological magnesium (Mg2+) concentrations.
To characterize the non-native structural states of the bI5 RNA.
To differentiate the observed collapsed state from known kinetic traps in RNA folding.

Main Methods:

Analysis of global RNA size at varying Mg2+ concentrations.
Determination of activation energy for folding from the collapsed state.

Related Experiment Videos

Assessment of urea's effect on the folding reaction.

Main Results:

The bI5 RNA catalytic core does not achieve its native structure at physiological Mg2+ levels.
RNA undergoes structural collapse at significantly lower Mg2+ concentrations than required for complete native folding.
An equilibrium exists between expanded and collapsed non-native states.
Folding from the collapsed state to the native state has negligible activation energy and is not urea-accelerated.
The collapsed state is distinct from kinetic traps seen in other large RNAs.

Conclusions:

The bI5 RNA forms a readily accessible collapsed non-native state.
This collapsed state may be a general intermediate preceding the assembly of ribonucleoprotein holoenzymes like the ribosome.