果蝇RNAi通路中siRNA结合蛋白dsRBD1和R2D2连接区域的化学位移定位。

IF 0.8 4区 生物学 Q4 BIOPHYSICS
Ramdas Aute, Mandar V. Deshmukh
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引用次数: 0

摘要

在模型生物果蝇中,Dicer同源物之一Dcr-2通过将长双链RNA切割成小干扰RNA(siRNA)来启动RNA干扰途径。Dcr-2:R2D2异二聚体随后与21个核苷酸的siRNA结合以形成R2D2:Dcr-2启动子(RDI)复合物,其对于启动包含引导siRNA链的RNA诱导沉默复合物的组装至关重要。在RDI复合物形成过程中,R2D2感知siRNA的5’端和5’-磷酸基团的稳定性,尽管R2D2对siRNA不对称感知和5’–磷酸识别的潜在机制尚不清楚。在这项研究中,我们提出了一种构建体的主链和侧链几乎完全的化学位移分配,该构建体包括R2D2的N-末端dsRBD1和接头(~ 10.3kDa;以下简称R2D2D1L)。我们的研究将进一步有助于R2D2的结构和功能表征。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Chemical shift assignments of dsRBD1 and linker region of R2D2, a siRNA binding protein in the Drosophila RNAi pathway

Chemical shift assignments of dsRBD1 and linker region of R2D2, a siRNA binding protein in the Drosophila RNAi pathway

In the model organism Drosophila melanogaster, one of the Dicer homologs, Dcr-2, initiates the RNA interference pathway by cleaving long double-stranded RNA into small interfering RNA (siRNA). The Dcr-2:R2D2 heterodimer subsequently binds to the 21-nucleotide siRNA to form the R2D2:Dcr-2 Initiator (RDI) complex, which is critical for initiating the assembly of the RNA-induced silencing complex containing guide siRNA strand. During RDI complex formation, R2D2 senses the stability of the 5′ end of the siRNA and a 5′-phosphate group, although the underlying mechanism of siRNA asymmetry sensing and 5′-phosphate recognition by R2D2 is elusive. In this study, we present nearly complete chemical shift assignments of the backbone and the side chain of a construct that comprises the N-terminus dsRBD1 and linker of R2D2 (~ 10.3 kDa; henceforth: R2D2D1L). Our study would further aid in the structural and functional characterization of R2D2.

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来源期刊
Biomolecular NMR Assignments
Biomolecular NMR Assignments 生物-光谱学
CiteScore
1.70
自引率
11.10%
发文量
59
审稿时长
6-12 weeks
期刊介绍: Biomolecular NMR Assignments provides a forum for publishing sequence-specific resonance assignments for proteins and nucleic acids as Assignment Notes. Chemical shifts for NMR-active nuclei in macromolecules contain detailed information on molecular conformation and properties. Publication of resonance assignments in Biomolecular NMR Assignments ensures that these data are deposited into a public database at BioMagResBank (BMRB; http://www.bmrb.wisc.edu/), where they are available to other researchers. Coverage includes proteins and nucleic acids; Assignment Notes are processed for rapid online publication and are published in biannual online editions in June and December.
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