Structural basis for RNA trimming by RNase T in stable RNA 3′-end maturation

被引：0

作者：

Hsiao Y.-Y. ^{[1
,2
]}

Yang C.-C. ^{[2
,3
]}

Lin C.L. ^{[1
,2
]}

Lin J.L.J. ^{[2
]}

Duh Y. ^{[2
]}

Yuan H.S. ^{[2
,3
]}

机构：

[1] Institute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu

[2] Institute of Molecular Biology, Academia Sinica, Taipei

[3] Graduate Institute of Biochemistry and Molecular Biology, National Taiwan University, Taipei

来源：

Nature Chemical Biology | 2011年 / 7卷 / 4期

关键词：

D O I：

10.1038/nchembio.524

中图分类号：

学科分类号：

摘要：

RNA maturation relies on various exonucleases to remove nucleotides successively from the 5′ or 3′ end of nucleic acids. However, little is known regarding the molecular basis for substrate and cleavage preference of exonucleases. Our biochemical and structural analyses on RNase T-DNA complexes show that the RNase T dimer has an ideal architecture for binding a duplex with a short 3′ overhang to produce a digestion product of a duplex with a 2-nucleotide (nt) or 1-nt 3′ overhang, depending on the composition of the last base pair in the duplex. A 'C-filter' in RNase T screens out the nucleic acids with 3′-terminal cytosines for hydrolysis by inducing a disruptive conformational change at the active site. Our results reveal the general principles and the working mechanism for the final trimming step made by RNase T in the maturation of stable RNA and pave the way for the understanding of other DEDD family exonucleases. © 2011 Nature America, Inc. All rights reserved.

引用

页码：236 / 243

页数：7

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