Elastic Coupling Between RNA Degradation and Unwinding by an Exoribonuclease

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Science  29 Jun 2012:
Vol. 336, Issue 6089, pp. 1726-1729
DOI: 10.1126/science.1216848

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To regulate cellular RNA levels, transcription must be balanced by RNA degradation. An important player is the exosome, which can unwind and degrade structured RNA. Lee et al. (p. 1726) used single-molecule fluorescence analysis to investigate how degradation and unwinding are coupled in the catalytic subunit of the yeast exosome complex, Rrp44. Rrp44 apparently digests several base pairs without unwinding, accumulates the energy, which it then uses to unwind four to five base pairs in a burst. Similar spring-like behavior has been proposed for conventional helicases, except that the stored energy comes from hydrolysis of adenosine triphosphate rather than the RNA polymer.


Rrp44 (Dis3) is a key catalytic subunit of the yeast exosome complex and can processively digest structured RNA one nucleotide at a time in the 3′ to 5′ direction. Its motor function is powered by the energy released from the hydrolytic nuclease reaction instead of adenosine triphosphate hydrolysis as in conventional helicases. Single-molecule fluorescence analysis revealed that instead of unwinding RNA in single base pair steps, Rrp44 accumulates the energy released by multiple single nucleotide step hydrolysis reactions until about four base pairs are unwound in a burst. Kinetic analyses showed that RNA unwinding, not cleavage or strand release, determines the overall RNA degradation rate and that the unwinding step size is determined by the nonlinear elasticity of the Rrp44/RNA complex, but not by duplex stability.

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