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10.1016/j.molcel.2015.07.006 http://scihub22266oqcxt.onion/10.1016/j.molcel.2015.07.006 C4560963!4560963!26257286     free     free     free Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Mol+Cell 2015 ; 59 (5): 807-18 Nephropedia Template TP {{tp|p=26257286|t=2015. TAF11 assembles RISC loading complex to enhance RNAi efficiency |pdf=|usr=}}{{26257286}} gab.com Text TAF11 assembles RISC loading complex to enhance RNAi efficiency JO: Mol Cell http://www.kidney.de/pget.php?&tw=1&pmid=26257286 #FOAvip Assembly of the RNA-induced silencing complex (RISC) requires formation of the RISC loading complex (RLC), which contains Dicer-2(Dcr-2)-R2D2 complex and recruits duplex siRNA to Ago2 in Drosophila melanogaster. However, the precise composition and action mechanism of Drosophila RLC remain unclear. Here, we identified the missing factor of RLC as TATA-binding protein associated factor 11 (TAF11) by genetic screen. Although an annotated nuclear transcription factor, we found that TAF11 also associated with Dcr-2/R2D2 and localized to cytoplasmic D2 bodies. Consistent with defective RLC assembly in taf11?/? ovary extract, we reconstituted the RLC in vitro using recombinant Dcr-2-R2D2 complex, TAF11, and duplex siRNA. Furthermore, we showed that TAF11 tetramer facilitates Dcr-2-R2D2 tetramerization to enhance siRNA binding and RISC loading activities. Together, our genetic and biochemical studies define the molecular nature of Drosophila RLC and elucidate a novel cytoplasmic function of TAF11 in organizing RLC assembly to enhance RNAi efficiency. Twit Text FOAVip TAF11 assembles RISC loading complex to enhance RNAi efficiency ????Mol Cell http://www.kidney.de/pget.php?&tw=1&pmid=26257286 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26257286 #FOAvip English Wikipedia <ref>{{Cite pmid|26257286}}</ref> TAF11 assembles RISC loading complex to enhance RNAi efficiency #MMPMID26257286 Liang C; Wang Y; Murota Y; Liu X; Smith D; Siomi MC; Liu Q Mol Cell 2015[Sep]; 59 (5): 807-18 PMID26257286show ga Assembly of the RNA-induced silencing complex (RISC) requires formation of the RISC loading complex (RLC), which contains Dicer-2(Dcr-2)-R2D2 complex and recruits duplex siRNA to Ago2 in Drosophila melanogaster. However, the precise composition and action mechanism of Drosophila RLC remain unclear. Here, we identified the missing factor of RLC as TATA-binding protein associated factor 11 (TAF11) by genetic screen. Although an annotated nuclear transcription factor, we found that TAF11 also associated with Dcr-2/R2D2 and localized to cytoplasmic D2 bodies. Consistent with defective RLC assembly in taf11?/? ovary extract, we reconstituted the RLC in vitro using recombinant Dcr-2-R2D2 complex, TAF11, and duplex siRNA. Furthermore, we showed that TAF11 tetramer facilitates Dcr-2-R2D2 tetramerization to enhance siRNA binding and RISC loading activities. Together, our genetic and biochemical studies define the molecular nature of Drosophila RLC and elucidate a novel cytoplasmic function of TAF11 in organizing RLC assembly to enhance RNAi efficiency. äTAF11 assembles RISC loading complex to enhance RNAi efficiency (epmc).pdf DeepDyve Pubget Overpricing