Molecular Recognition by Glycoside Pseudo Base Pairs and Triples in an Apramycin-RNA Complex

2005 ◽  
Vol 44 (18) ◽  
pp. 2694-2700 ◽  
Author(s):  
Qing Han ◽  
Qiang Zhao ◽  
Sarah Fish ◽  
Klaus B. Simonsen ◽  
Dionisios Vourloumis ◽  
...  
2005 ◽  
Vol 117 (18) ◽  
pp. 2754-2760 ◽  
Author(s):  
Qing Han ◽  
Qiang Zhao ◽  
Sarah Fish ◽  
Klaus B. Simonsen ◽  
Dionisios Vourloumis ◽  
...  

Science ◽  
2012 ◽  
Vol 336 (6089) ◽  
pp. 1726-1729 ◽  
Author(s):  
Gwangrog Lee ◽  
Matthew A. Bratkowski ◽  
Fang Ding ◽  
Ailong Ke ◽  
Taekjip Ha

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.


Nature ◽  
2003 ◽  
Vol 426 (6962) ◽  
pp. 96-100 ◽  
Author(s):  
Duo Lu ◽  
M. Alexandra Searles ◽  
Aaron Klug

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