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Volumn 20, Issue 3, 2013, Pages 380-386

Structural basis for duplex RNA recognition and cleavage by Archaeoglobus fulgidus C3PO

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; C3PO PROTEIN; RNA; UNCLASSIFIED DRUG;

EID: 84875217890     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.2487     Document Type: Article
Times cited : (14)

References (54)
  • 1
    • 58449134534 scopus 로고    scopus 로고
    • Small silencing RNAs: An expanding universe
    • Ghildiyal, M. & Zamore, P.D. Small silencing RNAs: an expanding universe. Nat. Rev. Genet. 10, 94-108 (2009).
    • (2009) Nat. Rev. Genet , vol.10 , pp. 94-108
    • Ghildiyal, M.1    Zamore, P.D.2
  • 3
    • 78650306521 scopus 로고    scopus 로고
    • Small RNA sorting: Matchmaking for Argonautes
    • Czech, B. & Hannon, G.J. Small RNA sorting: matchmaking for Argonautes. Nat. Rev. Genet. 12, 19-31 (2011).
    • (2011) Nat. Rev. Genet , vol.12 , pp. 19-31
    • Czech, B.1    Hannon, G.J.2
  • 5
    • 0035798415 scopus 로고    scopus 로고
    • ATP requirements and small interfering RNA structure in the RNA interference pathway
    • Nykänen, A., Haley, B. & Zamore, P.D. ATP requirements and small interfering RNA 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
  • 6
    • 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
  • 7
    • 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
  • 8
    • 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. Nat. Struct. Mol. Biol. 16, 953-960 (2009).
    • (2009) Nat. Struct. Mol. Biol , vol.16 , pp. 953-960
    • Kawamata, T.1    Seitz, H.2    Tomari, Y.3
  • 9
    • 77449128456 scopus 로고    scopus 로고
    • ATP-dependent human RISC assembly pathways
    • Yoda, M. et al. ATP-dependent human RISC assembly pathways. Nat. Struct. Mol. Biol. 17, 17-23 (2010).
    • (2010) Nat. Struct. Mol. Biol , vol.17 , pp. 17-23
    • Yoda, M.1
  • 10
    • 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
  • 11
    • 77955426711 scopus 로고    scopus 로고
    • A direct role for Hsp90 in pre-RISC formation in Drosophila
    • Miyoshi, T., Takeuchi, A., Siomi, H. & Siomi, M.C. A direct role for Hsp90 in pre-RISC formation in Drosophila. Nat. Struct. Mol. Biol. 17, 1024-1026 (2010).
    • (2010) Nat. Struct. Mol. Biol , vol.17 , pp. 1024-1026
    • Miyoshi, T.1    Takeuchi, A.2    Siomi, H.3    Siomi, M.C.4
  • 12
    • 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
  • 13
    • 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
  • 14
    • 1842816517 scopus 로고    scopus 로고
    • Distinct roles for Drosophila Dicer-1 and Dicer-2 in the siRNA/miRNA silencing pathways
    • Lee, Y.S. et al. Distinct roles for Drosophila Dicer-1 and Dicer-2 in the siRNA/miRNA silencing pathways. Cell 117, 69-81 (2004).
    • (2004) Cell , vol.117 , pp. 69-81
    • Lee, Y.S.1
  • 15
    • 33746581711 scopus 로고    scopus 로고
    • Dicer-2 and R2D2 coordinately bind siRNA to promote assembly of the siRISC complexes
    • Liu, X., Jiang, F., Kalidas, S., Smith, D. & Liu, Q. Dicer-2 and R2D2 coordinately bind siRNA to promote assembly of the siRISC complexes. RNA 12, 1514-1520 (2006).
    • (2006) RNA , vol.12 , pp. 1514-1520
    • Liu, X.1    Jiang, F.2    Kalidas, S.3    Smith, D.4    Liu, Q.5
  • 16
    • 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
  • 17
    • 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. Nat. Struct. Mol. Biol. 18, 650-657 (2011).
    • (2011) Nat. Struct. Mol. Biol , vol.18 , pp. 650-657
    • Ye, X.1
  • 18
    • 10744225153 scopus 로고    scopus 로고
    • Asymmetry in the assembly of the RNAi enzyme complex
    • Schwarz, D.S. et al. Asymmetry in the assembly of the RNAi enzyme complex. Cell 115, 199-208 (2003).
    • (2003) Cell , vol.115 , pp. 199-208
    • Schwarz, D.S.1
  • 19
    • 0142165224 scopus 로고    scopus 로고
    • Functional siRNAs and miRNAs exhibit strand bias
    • Khvorova, A., Reynolds, A. & Jayasena, S.D. Functional siRNAs and miRNAs exhibit strand bias. Cell 115, 209-216 (2003).
    • (2003) Cell , vol.115 , pp. 209-216
    • Khvorova, A.1    Reynolds, A.2    Jayasena, S.D.3
  • 20
    • 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
  • 21
    • 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
  • 22
    • 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
  • 23
    • 33645763485 scopus 로고    scopus 로고
    • Cleavage of the siRNA passenger strand during RISC assembly in human cells
    • Leuschner, P.J., Ameres, S.L., Kueng, S. & Martinez, J. Cleavage of the siRNA passenger strand during RISC assembly in human cells. EMBO Rep. 7, 314-320 (2006).
    • (2006) EMBO Rep , vol.7 , pp. 314-320
    • Leuschner, P.J.1    Ameres, S.L.2    Kueng, S.3    Martinez, J.4
  • 24
    • 56249145105 scopus 로고    scopus 로고
    • Structure of the guide-strand-containing argonaute silencing complex
    • Wang, Y., Sheng, G., Juranek, S., Tuschl, T. & Patel, D.J. Structure of the guide-strand-containing argonaute silencing complex. Nature 456, 209-213 (2008).
    • (2008) Nature , vol.456 , pp. 209-213
    • Wang, Y.1    Sheng, G.2    Juranek, S.3    Tuschl, T.4    Patel, D.J.5
  • 25
    • 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
  • 27
    • 84863624199 scopus 로고    scopus 로고
    • The structure of human Argonaute-2 in complex with miR-20a
    • Elkayam, E. et al. The structure of human Argonaute-2 in complex with miR-20a. Cell 150, 100-110 (2012).
    • (2012) Cell , vol.150 , pp. 100-110
    • Elkayam, E.1
  • 28
    • 77954700065 scopus 로고    scopus 로고
    • Biological roles of translin and translin-associated factor-X: RNA metabolism comes to the fore
    • Jaendling, A. & McFarlane, R.J. Biological roles of translin and translin-associated factor-X: RNA metabolism comes to the fore. Biochem. J. 429, 225-234 (2010).
    • (2010) Biochem. J , vol.429 , pp. 225-234
    • Jaendling, A.1    McFarlane, R.J.2
  • 29
    • 84864690535 scopus 로고    scopus 로고
    • The translin-TRAX complex (C3PO) is a ribonuclease in tRNA processing
    • Li, L. et al. The translin-TRAX complex (C3PO) is a ribonuclease in tRNA processing. Nat. Struct. Mol. Biol. 19, 824-830 (2012).
    • (2012) Nat. Struct. Mol. Biol , vol.19 , pp. 824-830
    • Li, L.1
  • 30
    • 79958819183 scopus 로고    scopus 로고
    • Multimeric assembly and biochemical characterization of the Trax-translin endonuclease complex
    • Tian, Y. et al. Multimeric assembly and biochemical characterization of the Trax-translin endonuclease complex. Nat. Struct. Mol. Biol. 18, 658-664 (2011).
    • (2011) Nat. Struct. Mol. Biol , vol.18 , pp. 658-664
    • Tian, Y.1
  • 31
    • 0036301351 scopus 로고    scopus 로고
    • Crystal structure of TB-RBP, a novel RNA-binding and regulating protein
    • Pascal, J.M., Hart, P.J., Hecht, N.B. & Robertus, J.D. Crystal structure of TB-RBP, a novel RNA-binding and regulating protein. J. Mol. Biol. 319, 1049-1057 (2002).
    • (2002) J. Mol. Biol , vol.319 , pp. 1049-1057
    • Pascal, J.M.1    Hart, P.J.2    Hecht, N.B.3    Robertus, J.D.4
  • 32
    • 8544237925 scopus 로고    scopus 로고
    • Structure of human translin at 2.2 Å resolution
    • Sugiura, I. et al. Structure of human translin at 2.2 Å resolution. Acta Crystallogr. D Biol. Crystallogr. 60, 674-679 (2004).
    • (2004) Acta Crystallogr. D Biol. Crystallogr , vol.60 , pp. 674-679
    • Sugiura, I.1
  • 33
    • 0042190668 scopus 로고    scopus 로고
    • Mice deficient for testis-brain RNA-binding protein exhibit a coordinate loss of TRAX, reduced fertility, altered gene expression in the brain, and behavioral changes
    • Chennathukuzhi, V. et al. Mice deficient for testis-brain RNA-binding protein exhibit a coordinate loss of TRAX, reduced fertility, altered gene expression in the brain, and behavioral changes. Mol. Cell. Biol. 23, 6419-6434 (2003).
    • (2003) Mol. Cell. Biol , vol.23 , pp. 6419-6434
    • Chennathukuzhi, V.1
  • 34
    • 1842477453 scopus 로고    scopus 로고
    • Translin-associated factor X is post-transcriptionally regulated by its partner protein TB-RBP, and both are essential for normal cell proliferation
    • Yang, S. et al. Translin-associated factor X is post-transcriptionally regulated by its partner protein TB-RBP, and both are essential for normal cell proliferation. J. Biol. Chem. 279, 12605-12614 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 12605-12614
    • Yang, S.1
  • 35
    • 20444387996 scopus 로고    scopus 로고
    • Co-expressed recombinant human Translin-Trax complex binds DNA
    • Gupta, G.D. et al. Co-expressed recombinant human Translin-Trax complex binds DNA. FEBS Lett. 579, 3141-3146 (2005).
    • (2005) FEBS Lett , vol.579 , pp. 3141-3146
    • Gupta, G.D.1
  • 36
    • 33751312484 scopus 로고    scopus 로고
    • Functional characterization of Drosophila Translin and Trax
    • Claussen, M., Koch, R., Jin, Z.Y. & Suter, B. Functional characterization of Drosophila Translin and Trax. Genetics 174, 1337-1347 (2006).
    • (2006) Genetics , vol.174 , pp. 1337-1347
    • Claussen, M.1    Koch, R.2    Jin, Z.Y.3    Suter, B.4
  • 37
    • 38349106272 scopus 로고    scopus 로고
    • Functional characterisation of the Schizosaccharomyces pombe homologue of the leukaemia-associated translocation breakpoint binding protein translin and its binding partner, TRAX
    • Jaendling, A., Ramayah, S., Pryce, D.W. & McFarlane, R.J. Functional characterisation of the Schizosaccharomyces pombe homologue of the leukaemia-associated translocation breakpoint binding protein translin and its binding partner, TRAX. Biochim. Biophys. Acta 1783, 203-213 (2008).
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 203-213
    • Jaendling, A.1    Ramayah, S.2    Pryce, D.W.3    McFarlane, R.J.4
  • 38
    • 0033039595 scopus 로고    scopus 로고
    • The DNA binding activity of Translin is mediated by a basic region in the ring-shaped structure conserved in evolution
    • Aoki, K., Suzuki, K., Ishida, R. & Kasai, M. The DNA binding activity of Translin is mediated by a basic region in the ring-shaped structure conserved in evolution. FEBS Lett. 443, 363-366 (1999).
    • (1999) FEBS Lett , vol.443 , pp. 363-366
    • Aoki, K.1    Suzuki, K.2    Ishida, R.3    Kasai, M.4
  • 39
    • 0035918307 scopus 로고    scopus 로고
    • Trax (translin-associated factor X), a primarily cytoplasmic protein, inhibits the binding of TB-RBP (translin) to RNA
    • Chennathukuzhi, V.M., Kurihara, Y., Bray, J.D. & Hecht, N.B. Trax (translin-associated factor X), a primarily cytoplasmic protein, inhibits the binding of TB-RBP (translin) to RNA. J. Biol. Chem. 276, 13256-13263 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 13256-13263
    • Chennathukuzhi, V.M.1    Kurihara, Y.2    Bray, J.D.3    Hecht, N.B.4
  • 40
    • 77953265216 scopus 로고    scopus 로고
    • Mapping of interaction sites of the Schizosaccharomyces pombe protein Translin with nucleic acids and proteins: A combined molecular genetics and bioinformatics study
    • Eliahoo, E. et al. Mapping of interaction sites of the Schizosaccharomyces pombe protein Translin with nucleic acids and proteins: a combined molecular genetics and bioinformatics study. Nucleic Acids Res. 38, 2975-2989 (2010).
    • (2010) Nucleic Acids Res , vol.38 , pp. 2975-2989
    • Eliahoo, E.1
  • 41
    • 84858052535 scopus 로고    scopus 로고
    • Identification of nucleic acid binding sites on translin-associated factor X (TRAX) protein
    • Gupta, G.D. & Kumar, V. Identification of nucleic acid binding sites on translin-associated factor X (TRAX) protein. PLoS ONE 7, e33035 (2012).
    • (2012) PLoS ONE , vol.7
    • Gupta, G.D.1    Kumar, V.2
  • 42
    • 0027390731 scopus 로고
    • Chemically modified RNA: Approaches and applications
    • Heidenreich, O., Pieken, W. & Eckstein, F. Chemically modified RNA: approaches and applications. FASEB J. 7, 90-96 (1993).
    • (1993) FASEB J , vol.7 , pp. 90-96
    • Heidenreich, O.1    Pieken, W.2    Eckstein, F.3
  • 43
    • 11244279683 scopus 로고    scopus 로고
    • Crystal structure of a PIWI protein suggests mechanisms for siRNA recognition and slicer activity
    • Parker, J.S., Roe, S.M. & Barford, D. Crystal structure of a PIWI protein suggests mechanisms for siRNA recognition and slicer activity. EMBO J. 23, 4727-4737 (2004).
    • (2004) EMBO J , vol.23 , pp. 4727-4737
    • Parker, J.S.1    Roe, S.M.2    Barford, D.3
  • 44
    • 75649151032 scopus 로고    scopus 로고
    • Xia2: An expert system for macromolecular crystallography data reduction
    • Winter, G. xia2: an expert system for macromolecular crystallography data reduction. J. Appl. Crystallogr. 43, 186-190 (2010).
    • (2010) J. Appl. Crystallogr , vol.43 , pp. 186-190
    • Winter, G.1
  • 46
    • 79953747244 scopus 로고    scopus 로고
    • An introduction to data reduction: Space-group determination, scaling and intensity statistics
    • Evans, P.R. An introduction to data reduction: space-group determination, scaling and intensity statistics. Acta Crystallogr. D Biol. Crystallogr. 67, 282-292 (2011).
    • (2011) Acta Crystallogr. D Biol. Crystallogr , vol.67 , pp. 282-292
    • Evans, P.R.1
  • 47
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project. N
    • Collaborative Computational Project. N. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D Biol. Crystallogr , vol.50 , pp. 760-763
  • 48
    • 0001763933 scopus 로고    scopus 로고
    • Difference structure-factor normalization for heavy-atom or anomalous-scattering substructure determinations
    • Blessing, R.H. & Smith, G.D. Difference structure-factor normalization for heavy-atom or anomalous-scattering substructure determinations. J. Appl. Crystallogr. 32, 664-670 (1999).
    • (1999) J. Appl. Crystallogr , vol.32 , pp. 664-670
    • Blessing, R.H.1    Smith, G.D.2
  • 49
    • 19944409045 scopus 로고    scopus 로고
    • The design and implementation of SnB v2.0
    • Weeks, C.M. & Miller, R. The design and implementation of SnB v2.0. J. Appl. Crystallogr. 32, 120-124 (1999).
    • (1999) J. Appl. Crystallogr , vol.32 , pp. 120-124
    • Weeks, C.M.1    Miller, R.2
  • 51
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P.D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66, 213-221 (2010).
    • (2010) Acta Crystallogr. D Biol. Crystallogr , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 53
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A.J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658-674 (2007).
    • (2007) J. Appl. Crystallogr , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 54
    • 65349114255 scopus 로고    scopus 로고
    • ALINE: A WYSIWYG protein-sequence alignment editor for publication-quality alignments
    • Bond, C.S. & Schuttelkopf, A.W. ALINE: a WYSIWYG protein-sequence alignment editor for publication-quality alignments. Acta Crystallogr. D Biol. Crystallogr. 65, 510-512 (2009).
    • (2009) Acta Crystallogr. D Biol. Crystallogr , vol.65 , pp. 510-512
    • Bond, C.S.1    Schuttelkopf, A.W.2


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