期刊
BIOCHEMISTRY
卷 55, 期 38, 页码 5321-5325出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.biochem.6b00849
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资金
- Vanderbilt University
RNase H1 cleaves the RNA strand of RNA:DNA hybrids. Replacement of RNA 2'-hydroxyls by fluorine (FRNA) is commonly used to stabilize aptamers and siRNAs. However, FRNA:DNA hybrids fail to elicit RNase H activity. The underlying reasons are unclear, as 2'-OH groups are not directly involved in cleavage. We determined the crystal structure of Bacillus halodurans RNase H bound to a FRNA:DNA hybrid. The structure points to dynamic (slippage of the FRNA:DNA hybrid relative to the enzyme), geometric (different Curvatures of FRNA:DNA and RNA:DNA hybrids), and electronic reasons (Mg2+ absent from the active site of the FRNA:DNA complex) for the loss of RNaseH activity.
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