메뉴 건너뛰기




Volumn 521, Issue 7553, 2015, Pages 533-536

Defining fundamental steps in the assembly of the Drosophila RNAi enzyme complex

Author keywords

[No Author keywords available]

Indexed keywords

5' PHOSPHATE; ARGONAUTE 2 PROTEIN; CHAPERONE; DICER; DICER 2; DROJ2 PROTEIN; HEAT SHOCK COGNATE PROTEIN 70; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 90; HOP PROTEIN; PHOSPHATE; PROTEIN P23; SMALL INTERFERING RNA; UNCLASSIFIED DRUG; AGO2 PROTEIN, DROSOPHILA; ARGONAUTE PROTEIN; DCR-2 PROTEIN, DROSOPHILA; DROSOPHILA PROTEIN; GUIDE RNA; HEAT SHOCK PROTEIN; HOPSCOTCH PROTEIN, DROSOPHILA; JANUS KINASE; PROTEIN BINDING; R2D2 PROTEIN, DROSOPHILA; RIBONUCLEASE III; RNA BINDING PROTEIN; RNA HELICASE; RNA INDUCED SILENCING COMPLEX; TRANSCRIPTION FACTOR;

EID: 84930643471     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature14254     Document Type: Article
Times cited : (106)

References (42)
  • 1
    • 60149088848 scopus 로고    scopus 로고
    • Origins andmechanisms ofmiRNAsand siRNAs
    • Carthew,R.W.&Sontheimer, E. J.Origins andmechanisms ofmiRNAsand siRNAs. Cell 136, 642-655 (2009).
    • (2009) Cell , vol.136 , pp. 642-655
    • Carthew, R.W.1    Sontheimer, E.J.2
  • 3
    • 0141868916 scopus 로고    scopus 로고
    • R2D2, a bridge between the initiation and effector steps of the Drosophila RNAi pathway
    • Liu, Q. et al. R2D2, a bridge between the initiation and effector steps of the Drosophila RNAi pathway. Science 301, 1921-1925 (2003).
    • (2003) Science , vol.301 , pp. 1921-1925
    • Liu, Q.1
  • 4
    • 1842766252 scopus 로고    scopus 로고
    • Dicer-2-dependent 80S complex cleaves targeted mRNAs during RNAi in Drosophila
    • Pham, J. W., Pellino, J. L., Lee, Y. S., Carthew, R. W. & Sontheimer, E. J. A. Dicer-2-dependent 80S complex cleaves targeted mRNAs during RNAi in Drosophila. Cell 117, 83-94 (2004).
    • (2004) Cell , vol.117 , pp. 83-94
    • Pham, J.W.1    Pellino, J.L.2    Lee, Y.S.3    Carthew, R.W.4    Sontheimer, E.J.A.5
  • 5
    • 1642603943 scopus 로고    scopus 로고
    • RISC assembly defects in the Drosophila RNAi mutant armitage
    • Tomari, Y. et al. RISC assembly defects in the Drosophila RNAi mutant armitage. Cell 116, 831-841 (2004).
    • (2004) Cell , vol.116 , pp. 831-841
    • Tomari, Y.1
  • 6
    • 77955479987 scopus 로고    scopus 로고
    • Vitro assembly of plant RNA-induced silencing complexes facilitated by molecular chaperone HSP90
    • Iki, T. et al. In vitro assembly of plant RNA-induced silencing complexes facilitated by molecular chaperone HSP90. Mol. Cell 39, 282-291 (2010).
    • (2010) Mol. Cell , vol.39 , pp. 282-291
    • Iki, T.1
  • 7
    • 77955478739 scopus 로고    scopus 로고
    • Hsc70/Hsp90 chaperone machinery mediates ATP-dependent RISC loading of small RNA duplexes
    • Iwasaki, S. et al. Hsc70/Hsp90 chaperone machinery mediates ATP-dependent RISC loading of small RNA duplexes. Mol. Cell 39, 292-299 (2010).
    • (2010) Mol. Cell , vol.39 , pp. 292-299
    • Iwasaki, S.1
  • 9
    • 69949127421 scopus 로고    scopus 로고
    • Structural determinants of miRNAs for RISC loading and slicer-independent unwinding
    • Kawamata, T., Seitz, H. & Tomari, Y. Structural determinants of miRNAs for RISC loading and slicer-independent unwinding. Nature Struct. Mol. Biol. 16, 953-960 (2009).
    • (2009) Nature Struct. Mol. Biol. , vol.16 , pp. 953-960
    • Kawamata, T.1    Seitz, H.2    Tomari, Y.3
  • 10
    • 13844294261 scopus 로고    scopus 로고
    • Dicer-deficient mouse embryonic stem cells are defective in differentiation and centromeric silencing
    • Kanellopoulou, C. et al. Dicer-deficient mouse embryonic stem cells are defective in differentiation and centromeric silencing. Genes Dev. 19, 489-501 (2005).
    • (2005) Genes Dev. , vol.19 , pp. 489-501
    • Kanellopoulou, C.1
  • 12
    • 79958825213 scopus 로고    scopus 로고
    • Structure of C3PO and mechanism of human RISC activation
    • Ye, X. et al. Structure of C3PO and mechanism of human RISC activation. Nature Struct. Mol. Biol. 18, 650-657 (2011).
    • (2011) Nature Struct. Mol. Biol. , vol.18 , pp. 650-657
    • Ye, X.1
  • 13
    • 84055222215 scopus 로고    scopus 로고
    • Dicer is dispensable for asymmetric RISC loading in mammals
    • Betancur, J. G. & Tomari, Y. Dicer is dispensable for asymmetric RISC loading in mammals. RNA 18, 24-30 (2012).
    • (2012) RNA , vol.18 , pp. 24-30
    • Betancur, J.G.1    Tomari, Y.2
  • 14
    • 84919705851 scopus 로고    scopus 로고
    • Deletion of human tarbp2 reveals cellular microRNA targets and cell-cycle function of TRBP
    • Kim, Y. et al. Deletion of human tarbp2 reveals cellular microRNA targets and cell-cycle function of TRBP. Cell Rep. 9, 1061-1074 (2014).
    • (2014) Cell Rep. , vol.9 , pp. 1061-1074
    • Kim, Y.1
  • 15
    • 77449128456 scopus 로고    scopus 로고
    • ATP-dependent human RISCassembly pathways
    • Yoda, M. et al. ATP-dependent human RISCassembly pathways. Nature Struct.Mol. Biol. 17, 17-23 (2010).
    • (2010) Nature Struct.Mol. Biol. , vol.17 , pp. 17-23
    • Yoda, M.1
  • 16
    • 77951712353 scopus 로고    scopus 로고
    • HSP90 protein stabilizes unloaded argonaute complexes and microscopic P-bodies in human cells
    • Johnston, M., Geoffroy, M. C., Sobala, A., Hay, R. & Hutvagner, G. HSP90 protein stabilizes unloaded argonaute complexes and microscopic P-bodies in human cells. Mol. Biol. Cell 21, 1462-1469 (2010).
    • (2010) Mol. Biol. Cell , vol.21 , pp. 1462-1469
    • Johnston, M.1    Geoffroy, M.C.2    Sobala, A.3    Hay, R.4    Hutvagner, G.5
  • 17
    • 27744590896 scopus 로고    scopus 로고
    • Passenger-strand cleavage facilitates assembly of siRNA into Ago2-containing RNAi enzyme complexes
    • Matranga, C., Tomari, Y., Shin, C., Bartel, D. P. & Zamore, P. D. Passenger-strand cleavage facilitates assembly of siRNA into Ago2-containing RNAi enzyme complexes. Cell 123, 607-620 (2005).
    • (2005) Cell , vol.123 , pp. 607-620
    • Matranga, C.1    Tomari, Y.2    Shin, C.3    Bartel, D.P.4    Zamore, P.D.5
  • 18
    • 28444437427 scopus 로고    scopus 로고
    • Slicer function of Drosophila Argonautes and its involvement in RISC formation
    • Miyoshi, K., Tsukumo, H., Nagami, T., Siomi, H. & Siomi, M. C. Slicer function of Drosophila Argonautes and its involvement in RISC formation. Genes Dev. 19, 2837-2848 (2005).
    • (2005) Genes Dev. , vol.19 , pp. 2837-2848
    • Miyoshi, K.1    Tsukumo, H.2    Nagami, T.3    Siomi, H.4    Siomi, M.C.5
  • 19
    • 27744506761 scopus 로고    scopus 로고
    • Argonaute2 cleaves the anti-guide strand of siRNA during RISC activation
    • Rand, T. A., Petersen, S.,Du, F.&Wang, X.Argonaute2 cleaves the anti-guide strand of siRNA during RISC activation. Cell 123, 621-629 (2005).
    • (2005) Cell , vol.123 , pp. 621-629
    • Rand, T.A.1    Petersen, S.2    Du, F.3    Wang, X.4
  • 20
    • 68449090733 scopus 로고    scopus 로고
    • C3PO, an endoribonuclease that promotes RNAi by facilitating RISC activation
    • Liu, Y. et al. C3PO, an endoribonuclease that promotes RNAi by facilitating RISC activation. Science 325, 750-753 (2009).
    • (2009) Science , vol.325 , pp. 750-753
    • Liu, Y.1
  • 21
    • 52949139464 scopus 로고    scopus 로고
    • The intersection of steroid receptors with molecular chaperones: Observations and questions
    • Smith, D. F. & Toft, D. O. The intersection of steroid receptors with molecular chaperones: observations and questions. Mol. Endocrinol. 22, 2229-2240 (2008).
    • (2008) Mol. Endocrinol. , vol.22 , pp. 2229-2240
    • Smith, D.F.1    Toft, D.O.2
  • 22
    • 79953682552 scopus 로고    scopus 로고
    • Phosphorylation of human Argonaute proteins affects small RNA binding
    • Rü del, S. et al. Phosphorylation of human Argonaute proteins affects small RNA binding. Nucleic Acids Res. 39, 2330-2343 (2011).
    • (2011) Nucleic Acids Res. , vol.39 , pp. 2330-2343
    • Rü Del, S.1
  • 23
    • 0030989277 scopus 로고    scopus 로고
    • Folding of the glucocorticoid receptor by the reconstituted Hsp90-based chaperone machinery. The initial hsp90.p60.hsp70-dependent step is sufficient for creating the steroid binding conformation
    • Dittmar, K. D. & Pratt, W. B. Folding of the glucocorticoid receptor by the reconstituted Hsp90-based chaperone machinery. The initial hsp90.p60.hsp70-dependent step is sufficient for creating the steroid binding conformation. J. Biol. Chem. 272, 13047-13054 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 13047-13054
    • Dittmar, K.D.1    Pratt, W.B.2
  • 24
    • 84883410514 scopus 로고    scopus 로고
    • Highly complementary target RNAs promote release of guide RNAs from human Argonaute2
    • De, N. et al. Highly complementary target RNAs promote release of guide RNAs from human Argonaute2. Mol. Cell 50, 344-355 (2013).
    • (2013) Mol. Cell , vol.50 , pp. 344-355
    • De, N.1
  • 25
  • 26
    • 84861451595 scopus 로고    scopus 로고
    • The crystal structure of human Argonaute2
    • Schirle, N. T. & MacRae, I. J. The crystal structure of human Argonaute2. Science 336, 1037-1040 (2012).
    • (2012) Science , vol.336 , pp. 1037-1040
    • Schirle, N.T.1    Macrae, I.J.2
  • 28
    • 0025100372 scopus 로고
    • Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein
    • Flaherty, K. M., DeLuca-Flaherty, C. & McKay, D. B. Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein. Nature 346, 623-628 (1990).
    • (1990) Nature , vol.346 , pp. 623-628
    • Flaherty, K.M.1    Deluca-Flaherty, C.2    McKay, D.B.3
  • 29
    • 0031444238 scopus 로고    scopus 로고
    • Identification and structural characterization of the ATP/ADPbinding site in the Hsp90 molecular chaperone
    • Prodromou, C. et al. Identification and structural characterization of the ATP/ADPbinding site in the Hsp90 molecular chaperone. Cell 90, 65-75 (1997).
    • (1997) Cell , vol.90 , pp. 65-75
    • Prodromou, C.1
  • 30
    • 75649106490 scopus 로고    scopus 로고
    • Strain through the neck linker ensures processive runs: A DNA-kinesin hybrid nanomachine study
    • Miyazono, Y., Hayashi, M., Karagiannis, P., Harada, Y. & Tadakuma, H. Strain through the neck linker ensures processive runs: a DNA-kinesin hybrid nanomachine study. EMBO J. 29, 93-106 (2010).
    • (2010) EMBO J. , vol.29 , pp. 93-106
    • Miyazono, Y.1    Hayashi, M.2    Karagiannis, P.3    Harada, Y.4    Tadakuma, H.5
  • 31
    • 0035798415 scopus 로고    scopus 로고
    • ATP requirements and small interferingRNA structure in the RNA interference pathway
    • Nykänen, A., Haley,B.&Zamore,P.D. ATP requirements and small interferingRNA structure in the RNA interference pathway. Cell 107, 309-321 (2001).
    • (2001) Cell , vol.107 , pp. 309-321
    • Nykänen, A.1    Haley, B.2    Zamore, P.D.3
  • 32
    • 0038387645 scopus 로고    scopus 로고
    • Vitro analysis of RNA interference in drosophila melanogaster
    • Haley, B., Tang,G.&Zamore, P.D. In vitro analysis ofRNAinterference in Drosophila melanogaster. Methods 30, 330-336 (2003).
    • (2003) Methods , vol.30 , pp. 330-336
    • Haley, B.1    Tang, G.2    Zamore, P.D.3
  • 33
    • 22744433240 scopus 로고    scopus 로고
    • Normal microRNA maturation and germ-line stem cell maintenance requires Loquacious, a double-stranded RNA-binding domain protein
    • Förstemann, K. et al. Normal microRNA maturation and germ-line stem cell maintenance requires Loquacious, a double-stranded RNA-binding domain protein. PLoS Biol. 3, e236 (2005).
    • (2005) PLoS Biol. , vol.3 , pp. e236
    • Förstemann, K.1
  • 34
    • 34447642555 scopus 로고    scopus 로고
    • Sorting of Drosophila small silencing RNAs
    • Tomari, Y., Du, T. & Zamore, P. D. Sorting of Drosophila small silencing RNAs. Cell 130, 299-308 (2007).
    • (2007) Cell , vol.130 , pp. 299-308
    • Tomari, Y.1    Du, T.2    Zamore, P.D.3
  • 35
    • 80051558967 scopus 로고    scopus 로고
    • Native gel analysis for RIS Cassembly
    • Kawamata, T.&Tomari, Y.Native gel analysis for RISCassembly.MethodsMol.Biol. 725, 91-105 (2011).
    • (2011) Methods Mol.Biol. , vol.725 , pp. 91-105
    • Kawamata, T.1    Tomari, Y.2
  • 36
    • 77953771590 scopus 로고    scopus 로고
    • AAA1 proteins RUVBL1 and RUVBL2 coordinate PIKK activity and function in nonsense-mediated mRNA decay
    • Izumi, N. et al. AAA1 proteins RUVBL1 and RUVBL2 coordinate PIKK activity and function in nonsense-mediated mRNA decay. Sci. Signal. 3, ra27 (2010).
    • (2010) Sci. Signal. , vol.3 , pp. ra27
    • Izumi, N.1
  • 37
    • 80455154961 scopus 로고    scopus 로고
    • Recognition of the pre-miRNA structure by Drosophila Dicer-1. Nature Struct
    • Tsutsumi, A., Kawamata, T., Izumi, N., Seitz, H. & Tomari, Y. Recognition of the pre-miRNA structure by Drosophila Dicer-1. Nature Struct. Mol. Biol. 18, 1153-1158 (2011).
    • (2011) Mol. Biol. , vol.18 , pp. 1153-1158
    • Tsutsumi, A.1    Kawamata, T.2    Izumi, N.3    Seitz, H.4    Tomari, Y.5
  • 38
    • 3042602447 scopus 로고    scopus 로고
    • Kinetic analysis of the RNAi enzyme complex
    • Haley, B. & Zamore, P. D. Kinetic analysis of the RNAi enzyme complex. Nature Struct. Mol. Biol. 11, 599-606 (2004).
    • (2004) Nature Struct. Mol. Biol. , vol.11 , pp. 599-606
    • Haley, B.1    Zamore, P.D.2
  • 39
    • 44949098384 scopus 로고    scopus 로고
    • Improved northern blotmethod for enhanced detection of small RNA
    • Pall, G. S.&Hamilton, A. J. Improved northern blotmethod for enhanced detection of small RNA. Nature Protocols 3, 1077-1084 (2008).
    • (2008) Nature Protocols , vol.3 , pp. 1077-1084
    • Pall, G.S.1    Hamilton, A.J.2
  • 40
    • 78149478349 scopus 로고    scopus 로고
    • Roles for the Yb body components Armitage and Yb in primary piRNA biogenesis in Drosophila
    • Saito, K. et al. Roles for the Yb body components Armitage and Yb in primary piRNA biogenesis in Drosophila. Genes Dev. 24, 2493-2498 (2010).
    • (2010) Genes Dev. , vol.24 , pp. 2493-2498
    • Saito, K.1
  • 41
    • 79955401564 scopus 로고    scopus 로고
    • Single molecule imaging of the trans-translation entry process via anchoring of the tagged ribosome
    • Zhou, Z. P. et al. Single molecule imaging of the trans-translation entry process via anchoring of the tagged ribosome. J. Biochem. 149, 609-618 (2011).
    • (2011) J. Biochem. , vol.149 , pp. 609-618
    • Zhou, Z.P.1
  • 42
    • 84857132597 scopus 로고    scopus 로고
    • Spatial organization of the extracellular matrix regulates cell-cell junction positioning
    • Tseng, Q. et al. Spatial organization of the extracellular matrix regulates cell-cell junction positioning. Proc. Natl Acad. Sci. USA 109, 1506-1511 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 1506-1511
    • Tseng, Q.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.