한빛사논문
- 조회4,815
Gwangrog Lee1,2, Matthew A. Bratkowski3, Fang Ding3, Ailong Ke3, Taekjip Ha1,4,*
1Department of Physics, University of Illinois at Urbana-Champaign, 1110 West Green Street, Urbana, IL 61801, USA. 2School of Life Sciences, Gwangju Institute of Science and Technology, Gwangju 500-712, Korea. 3Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853, USA. 4Howard Hughes Medical Institute, Urbana, IL 61801 USA.
*To whom correspondence should be addressed.
Abstract
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.
논문정보
- Research article
- 2012년 06월 (BRIC 등록일 )
- 국내+국외 연구진
- 생명과학 > 구조생물 및 생물물리학
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