TAF11 Assembles the RISC Loading Complex to Enhance RNAi Efficiency

Chunyang Liang, Yibing Wang, Yukiko Murota, Xiang Liu, Dean Smith, Mikiko C. Siomi, Qinghua Liu

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Assembly of the RNA-induced silencing complex (RISC) requires formation of the RISC loading complex (RLC), which contains the 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 it is 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<sup>-/-</sup> ovary extract, we reconstituted the RLC in vitro using the 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 the Drosophila RLC and elucidate a cytoplasmic function of TAF11 in organizing RLC assembly to enhance RNAi efficiency. Liang et al. show that TAF11, an annotated nuclear transcription factor, is part of the Drosophila RISC loading complex (RLC). They provide evidence that TAF11 assembles the RLC by facilitating Dcr-2-R2D2 tetramerization to enhance RNAi efficiency.

Original languageEnglish (US)
Pages (from-to)807-818
Number of pages12
JournalMolecular Cell
Volume59
Issue number5
DOIs
StatePublished - Sep 3 2015

Fingerprint

TATA-Binding Protein Associated Factors
RNA-Induced Silencing Complex
RNA Interference
Small Interfering RNA
Drosophila
Transcription Factors
Drosophila melanogaster
Molecular Biology
Ovary

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

Cite this

Liang, C., Wang, Y., Murota, Y., Liu, X., Smith, D., Siomi, M. C., & Liu, Q. (2015). TAF11 Assembles the RISC Loading Complex to Enhance RNAi Efficiency. Molecular Cell, 59(5), 807-818. https://doi.org/10.1016/j.molcel.2015.07.006

TAF11 Assembles the RISC Loading Complex to Enhance RNAi Efficiency. / Liang, Chunyang; Wang, Yibing; Murota, Yukiko; Liu, Xiang; Smith, Dean; Siomi, Mikiko C.; Liu, Qinghua.

In: Molecular Cell, Vol. 59, No. 5, 03.09.2015, p. 807-818.

Research output: Contribution to journalArticle

Liang, C, Wang, Y, Murota, Y, Liu, X, Smith, D, Siomi, MC & Liu, Q 2015, 'TAF11 Assembles the RISC Loading Complex to Enhance RNAi Efficiency', Molecular Cell, vol. 59, no. 5, pp. 807-818. https://doi.org/10.1016/j.molcel.2015.07.006
Liang, Chunyang ; Wang, Yibing ; Murota, Yukiko ; Liu, Xiang ; Smith, Dean ; Siomi, Mikiko C. ; Liu, Qinghua. / TAF11 Assembles the RISC Loading Complex to Enhance RNAi Efficiency. In: Molecular Cell. 2015 ; Vol. 59, No. 5. pp. 807-818.
@article{a02827ccfe1848de8835dda1c541a9ed,
title = "TAF11 Assembles the RISC Loading Complex to Enhance RNAi Efficiency",
abstract = "Assembly of the RNA-induced silencing complex (RISC) requires formation of the RISC loading complex (RLC), which contains the 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 it is 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 the 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 the Drosophila RLC and elucidate a cytoplasmic function of TAF11 in organizing RLC assembly to enhance RNAi efficiency. Liang et al. show that TAF11, an annotated nuclear transcription factor, is part of the Drosophila RISC loading complex (RLC). They provide evidence that TAF11 assembles the RLC by facilitating Dcr-2-R2D2 tetramerization to enhance RNAi efficiency.",
author = "Chunyang Liang and Yibing Wang and Yukiko Murota and Xiang Liu and Dean Smith and Siomi, {Mikiko C.} and Qinghua Liu",
year = "2015",
month = "9",
day = "3",
doi = "10.1016/j.molcel.2015.07.006",
language = "English (US)",
volume = "59",
pages = "807--818",
journal = "Molecular Cell",
issn = "1097-2765",
publisher = "Cell Press",
number = "5",

}

TY - JOUR

T1 - TAF11 Assembles the RISC Loading Complex to Enhance RNAi Efficiency

AU - Liang, Chunyang

AU - Wang, Yibing

AU - Murota, Yukiko

AU - Liu, Xiang

AU - Smith, Dean

AU - Siomi, Mikiko C.

AU - Liu, Qinghua

PY - 2015/9/3

Y1 - 2015/9/3

N2 - Assembly of the RNA-induced silencing complex (RISC) requires formation of the RISC loading complex (RLC), which contains the 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 it is 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 the 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 the Drosophila RLC and elucidate a cytoplasmic function of TAF11 in organizing RLC assembly to enhance RNAi efficiency. Liang et al. show that TAF11, an annotated nuclear transcription factor, is part of the Drosophila RISC loading complex (RLC). They provide evidence that TAF11 assembles the RLC by facilitating Dcr-2-R2D2 tetramerization to enhance RNAi efficiency.

AB - Assembly of the RNA-induced silencing complex (RISC) requires formation of the RISC loading complex (RLC), which contains the 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 it is 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 the 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 the Drosophila RLC and elucidate a cytoplasmic function of TAF11 in organizing RLC assembly to enhance RNAi efficiency. Liang et al. show that TAF11, an annotated nuclear transcription factor, is part of the Drosophila RISC loading complex (RLC). They provide evidence that TAF11 assembles the RLC by facilitating Dcr-2-R2D2 tetramerization to enhance RNAi efficiency.

UR - http://www.scopus.com/inward/record.url?scp=84940890444&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84940890444&partnerID=8YFLogxK

U2 - 10.1016/j.molcel.2015.07.006

DO - 10.1016/j.molcel.2015.07.006

M3 - Article

C2 - 26257286

AN - SCOPUS:84940890444

VL - 59

SP - 807

EP - 818

JO - Molecular Cell

JF - Molecular Cell

SN - 1097-2765

IS - 5

ER -