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Kinetic Intermediates Trapped by Native Interactions in RNA Folding

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Science  20 Mar 1998:
Vol. 279, Issue 5358, pp. 1943-1946
DOI: 10.1126/science.279.5358.1943

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Abstract

In the magnesium ion–dependent folding of theTetrahymena ribozyme, a kinetic intermediate accumulates in which the P4-P6 domain is formed, but the P3-P7 domain is not. The kinetic barriers to P3-P7 formation were investigated with the use of in vitro selection to identify mutant RNA molecules in which the folding rate of the P3-P7 domain was increased. The critical mutations disrupt native tertiary interactions within the P4-P6 domain and increase the rate of P3-P7 formation by destabilizing a kinetically trapped intermediate. Hence, kinetic traps stabilized by native interactions, and not simply by mispaired nonnative structures, can present a substantial barrier to RNA folding.

  • * Present address: Center for Cellular and Genetic Therapies, Department of Surgery, Duke University Medical Center, Durham, NC 27710, USA.

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