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Volumn 546, Issue 7660, 2017, Pages 617-621

Structure of a pre-catalytic spliceosome

Author keywords

[No Author keywords available]

Indexed keywords

B COMPLEX PROTEIN PRP38; B COMPLEX PROTEIN SNU23; B COMPLEX PROTEIN SPP381; HELICASE; MESSENGER RNA PRECURSOR; SMALL NUCLEAR RIBONUCLEOPROTEIN; UNCLASSIFIED DRUG; BRR2 PROTEIN, S CEREVISIAE; NUCLEAR PROTEIN; PROTEIN BINDING; PRP38 PROTEIN, S CEREVISIAE; PRP8 PROTEIN, S CEREVISIAE; RNA HELICASE; RNA PRECURSOR; RNA SPLICING FACTOR; SACCHAROMYCES CEREVISIAE PROTEIN; SMALL NUCLEAR RNA; SNU23 PROTEIN, S CEREVISIAE; SPP381 PROTEIN, S CEREVISIAE; U6 SMALL NUCLEAR RNA;

EID: 85021686355     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature22799     Document Type: Article
Times cited : (172)

References (76)
  • 2
    • 84977515240 scopus 로고    scopus 로고
    • A spliceosome intermediate with loosely associated tri-snRNP accumulates in the absence of Prp28 ATPase activity
    • Boesler, C. et al. A spliceosome intermediate with loosely associated tri-snRNP accumulates in the absence of Prp28 ATPase activity. Nat. Commun. 7, 11997 (2016).
    • (2016) Nat. Commun. , vol.7 , pp. 11997
    • Boesler, C.1
  • 3
    • 0033010430 scopus 로고    scopus 로고
    • An RNA switch at the 5' splice site requires ATP and the DEAD box protein Prp28p
    • Staley, J. P. & Guthrie, C. An RNA switch at the 5' splice site requires ATP and the DEAD box protein Prp28p. Mol. Cell 3, 55-64 (1999).
    • (1999) Mol. Cell , vol.3 , pp. 55-64
    • Staley, J.P.1    Guthrie, C.2
  • 4
    • 0027739852 scopus 로고
    • Mutations in U6 snRNA that alter splice site specificity: Implications for the active site
    • Lesser, C. F. & Guthrie, C. Mutations in U6 snRNA that alter splice site specificity: implications for the active site. Science 262, 1982-1988 (1993).
    • (1993) Science , vol.262 , pp. 1982-1988
    • Lesser, C.F.1    Guthrie, C.2
  • 5
    • 0032908071 scopus 로고    scopus 로고
    • Elevated levels of a U4/U6.U5 snRNP-associated protein, Spp381p, rescue a mutant defective in spliceosome maturation
    • Lybarger, S. et al. Elevated levels of a U4/U6.U5 snRNP-associated protein, Spp381p, rescue a mutant defective in spliceosome maturation. Mol. Cell. Biol. 19, 577-584 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 577-584
    • Lybarger, S.1
  • 6
    • 0033595016 scopus 로고    scopus 로고
    • Purification of the yeast U4/U6.U5 small nuclear ribonucleoprotein particle and identification of its proteins
    • Stevens, S. W. & Abelson, J. Purification of the yeast U4/U6.U5 small nuclear ribonucleoprotein particle and identification of its proteins. Proc. Natl Acad. Sci. USA 96, 7226-7231 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 7226-7231
    • Stevens, S.W.1    Abelson, J.2
  • 7
    • 0032515969 scopus 로고    scopus 로고
    • The human U5-200kD DEXH-box protein unwinds U4/U6 RNA duplices in vitro
    • Laggerbauer, B., Achsel, T. & Lührmann, R. The human U5-200kD DEXH-box protein unwinds U4/U6 RNA duplices in vitro. Proc. Natl Acad. Sci. USA 95, 4188-4192 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 4188-4192
    • Laggerbauer, B.1    Achsel, T.2    Lührmann, R.3
  • 8
    • 0032537739 scopus 로고    scopus 로고
    • RNA unwinding in U4/U6 snRNPs requires ATP hydrolysis and the DEIH-box splicing factor Brr2
    • Raghunathan, P. L. & Guthrie, C. RNA unwinding in U4/U6 snRNPs requires ATP hydrolysis and the DEIH-box splicing factor Brr2. Curr. Biol. 8, 847-855 (1998).
    • (1998) Curr. Biol. , vol.8 , pp. 847-855
    • Raghunathan, P.L.1    Guthrie, C.2
  • 9
    • 70449625597 scopus 로고    scopus 로고
    • The evolutionarily conserved core design of the catalytic activation step of the yeast spliceosome
    • Fabrizio, P. et al. The evolutionarily conserved core design of the catalytic activation step of the yeast spliceosome. Mol. Cell 36, 593-608 (2009).
    • (2009) Mol. Cell , vol.36 , pp. 593-608
    • Fabrizio, P.1
  • 10
    • 78649656777 scopus 로고    scopus 로고
    • Characterization of purified human Bact spliceosomal complexes reveals compositional and morphological changes during spliceosome activation and first step catalysis
    • Bessonov, S. et al. Characterization of purified human Bact spliceosomal complexes reveals compositional and morphological changes during spliceosome activation and first step catalysis. RNA 16, 2384-2403 (2010).
    • (2010) RNA , vol.16 , pp. 2384-2403
    • Bessonov, S.1
  • 11
    • 0028365538 scopus 로고
    • Functional association of essential splicing factor(s) with PRP19 in a protein complex
    • Tarn, W. Y. et al. Functional association of essential splicing factor(s) with PRP19 in a protein complex. EMBO J. 13, 2421-2431 (1994).
    • (1994) EMBO J. , vol.13 , pp. 2421-2431
    • Tarn, W.Y.1
  • 12
    • 84979516798 scopus 로고    scopus 로고
    • Single molecule analysis reveals reversible and irreversible steps during spliceosome activation
    • Hoskins, A. A., Rodgers, M. L., Friedman, L. J., Gelles, J. & Moore, M. J. Single molecule analysis reveals reversible and irreversible steps during spliceosome activation. eLife 5, e14166 (2016).
    • (2016) ELife , vol.5 , pp. e14166
    • Hoskins, A.A.1    Rodgers, M.L.2    Friedman, L.J.3    Gelles, J.4    Moore, M.J.5
  • 13
    • 0026486883 scopus 로고
    • A novel base-pairing interaction between U2 and U6 snRNAs suggests a mechanism for the catalytic activation of the spliceosome
    • Madhani, H. D. & Guthrie, C. A novel base-pairing interaction between U2 and U6 snRNAs suggests a mechanism for the catalytic activation of the spliceosome. Cell 71, 803-817 (1992).
    • (1992) Cell , vol.71 , pp. 803-817
    • Madhani, H.D.1    Guthrie, C.2
  • 14
    • 0027184481 scopus 로고
    • A general two-metal-ion mechanism for catalytic RNA
    • Steitz, T. A. & Steitz, J. A. A general two-metal-ion mechanism for catalytic RNA. Proc. Natl Acad. Sci. USA 90, 6498-6502 (1993).
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 6498-6502
    • Steitz, T.A.1    Steitz, J.A.2
  • 15
    • 84887624226 scopus 로고    scopus 로고
    • RNA catalyses nuclear pre-mRNA splicing
    • Fica, S. M. et al. RNA catalyses nuclear pre-mRNA splicing. Nature 503, 229-234 (2013).
    • (2013) Nature , vol.503 , pp. 229-234
    • Fica, S.M.1
  • 16
    • 0026605043 scopus 로고
    • U5 snRNA interacts with exon sequences at 5' and 3' splice sites
    • Newman, A. J. & Norman, C. U5 snRNA interacts with exon sequences at 5' and 3' splice sites. Cell 68, 743-754 (1992).
    • (1992) Cell , vol.68 , pp. 743-754
    • Newman, A.J.1    Norman, C.2
  • 17
    • 0027739853 scopus 로고
    • The U5 and U6 small nuclear RNAs as active site components of the spliceosome
    • Sontheimer, E. J. & Steitz, J. A. The U5 and U6 small nuclear RNAs as active site components of the spliceosome. Science 262, 1989-1996 (1993).
    • (1993) Science , vol.262 , pp. 1989-1996
    • Sontheimer, E.J.1    Steitz, J.A.2
  • 18
    • 84986612633 scopus 로고    scopus 로고
    • Cryo-EM structure of the spliceosome immediately after branching
    • Galej, W. P. et al. Cryo-EM structure of the spliceosome immediately after branching. Nature 537, 197-201 (2016).
    • (2016) Nature , vol.537 , pp. 197-201
    • Galej, W.P.1
  • 19
    • 84980369106 scopus 로고    scopus 로고
    • Structure of a yeast catalytic step i spliceosome at 3.4 Å resolution
    • Wan, R., Yan, C., Bai, R., Huang, G. & Shi, Y. Structure of a yeast catalytic step I spliceosome at 3.4 Å resolution. Science 353, 895-904 (2016).
    • (2016) Science , vol.353 , pp. 895-904
    • Wan, R.1    Yan, C.2    Bai, R.3    Huang, G.4    Shi, Y.5
  • 20
    • 84986581351 scopus 로고    scopus 로고
    • Molecular architecture of the Saccharomyces cerevisiae activated spliceosome
    • Rauhut, R. et al. Molecular architecture of the Saccharomyces cerevisiae activated spliceosome. Science 353, 1399-1405 (2016).
    • (2016) Science , vol.353 , pp. 1399-1405
    • Rauhut, R.1
  • 21
    • 84980378586 scopus 로고    scopus 로고
    • Structure of a yeast activated spliceosome at 3.5 Å resolution
    • Yan, C., Wan, R., Bai, R., Huang, G. & Shi, Y. Structure of a yeast activated spliceosome at 3.5 Å resolution. Science 353, 904-911 (2016).
    • (2016) Science , vol.353 , pp. 904-911
    • Yan, C.1    Wan, R.2    Bai, R.3    Huang, G.4    Shi, Y.5
  • 22
    • 85027950272 scopus 로고    scopus 로고
    • Structure of a yeast step II catalytically activated spliceosome
    • Yan, C., Wan, R., Bai, R., Huang, G. & Shi, Y. Structure of a yeast step II catalytically activated spliceosome. Science 355, 149-155 (2017).
    • (2017) Science , vol.355 , pp. 149-155
    • Yan, C.1    Wan, R.2    Bai, R.3    Huang, G.4    Shi, Y.5
  • 23
    • 85016141734 scopus 로고    scopus 로고
    • Structure of a spliceosome remodelled for exon ligation
    • Fica, S. M. et al. Structure of a spliceosome remodelled for exon ligation. Nature 542, 377-380 (2017).
    • (2017) Nature , vol.542 , pp. 377-380
    • Fica, S.M.1
  • 24
    • 85016153737 scopus 로고    scopus 로고
    • Cryo-EM structure of a human spliceosome activated for step 2 of splicing
    • Bertram, K. et al. Cryo-EM structure of a human spliceosome activated for step 2 of splicing. Nature 542, 318-323 (2017).
    • (2017) Nature , vol.542 , pp. 318-323
    • Bertram, K.1
  • 25
    • 84959322377 scopus 로고    scopus 로고
    • Molecular architecture of the human U4/U6.U5 tri-snRNP
    • Agafonov, D. E. et al. Molecular architecture of the human U4/U6.U5 tri-snRNP. Science 351, 1416-1420 (2016).
    • (2016) Science , vol.351 , pp. 1416-1420
    • Agafonov, D.E.1
  • 26
    • 84956686435 scopus 로고    scopus 로고
    • The 3.8 Å structure of the U4/U6.U5 tri-snRNP: Insights into spliceosome assembly and catalysis
    • Wan, R. et al. The 3.8 Å structure of the U4/U6.U5 tri-snRNP: insights into spliceosome assembly and catalysis. Science 351, 466-475 (2016).
    • (2016) Science , vol.351 , pp. 466-475
    • Wan, R.1
  • 27
    • 84958967476 scopus 로고    scopus 로고
    • Cryo-EM structure of the yeast U4/U6.U5 tri-snRNP at 3.7 Å resolution
    • Nguyen, T. H. D. et al. Cryo-EM structure of the yeast U4/U6.U5 tri-snRNP at 3.7 Å resolution. Nature 530, 298-302 (2016).
    • (2016) Nature , vol.530 , pp. 298-302
    • Nguyen, T.H.D.1
  • 28
    • 85019934461 scopus 로고    scopus 로고
    • Crystal structure of U2 snRNP SF3b components: Hsh49p in complex with Cus1p-binding domain
    • van Roon, A.-M. M. et al. Crystal structure of U2 snRNP SF3b components: Hsh49p in complex with Cus1p-binding domain. RNA 23, 968-981 (2017).
    • (2017) RNA , vol.23 , pp. 968-981
    • Van Roon, A.-M.M.1
  • 29
    • 84858800333 scopus 로고    scopus 로고
    • Structure and assembly of the SF3a splicing factor complex of U2 snRNP
    • Lin, P.-C. & Xu, R.-M. Structure and assembly of the SF3a splicing factor complex of U2 snRNP. EMBO J. 31, 1579-1590 (2012).
    • (2012) EMBO J. , vol.31 , pp. 1579-1590
    • Lin, P.-C.1    Xu, R.-M.2
  • 30
    • 84992091155 scopus 로고    scopus 로고
    • Molecular architecture of SF3b and structural consequences of its cancer-related mutations
    • Cretu, C. et al. Molecular architecture of SF3b and structural consequences of its cancer-related mutations. Mol. Cell 64, 307-319 (2016).
    • (2016) Mol. Cell , vol.64 , pp. 307-319
    • Cretu, C.1
  • 31
    • 84955170008 scopus 로고    scopus 로고
    • Protein localisation by electron microscopy reveals the architecture of the yeast spliceosomal B complex
    • Rigo, N., Sun, C., Fabrizio, P., Kastner, B. & Lührmann, R. Protein localisation by electron microscopy reveals the architecture of the yeast spliceosomal B complex. EMBO J. 34, 3059-3073 (2015).
    • (2015) EMBO J. , vol.34 , pp. 3059-3073
    • Rigo, N.1    Sun, C.2    Fabrizio, P.3    Kastner, B.4    Lührmann, R.5
  • 32
    • 2342539773 scopus 로고    scopus 로고
    • Three-dimensional structure of a pre-catalytic human spliceosomal complex B
    • Boehringer, D. et al. Three-dimensional structure of a pre-catalytic human spliceosomal complex B. Nat. Struct. Mol. Biol. 11, 463-468 (2004).
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 463-468
    • Boehringer, D.1
  • 33
    • 33745860086 scopus 로고    scopus 로고
    • Protein composition and electron microscopy structure of affinity-purified human spliceosomal B complexes isolated under physiological conditions
    • Deckert, J. et al. Protein composition and electron microscopy structure of affinity-purified human spliceosomal B complexes isolated under physiological conditions. Mol. Cell. Biol. 26, 5528-5543 (2006).
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 5528-5543
    • Deckert, J.1
  • 34
    • 0027491331 scopus 로고
    • Yeast precursor mRNA processing protein PRP19 associates with the spliceosome concomitant with or just after dissociation of U4 small nuclear RNA
    • Tarn, W.-Y., Lee, K.-R. & Cheng, S. C. Yeast precursor mRNA processing protein PRP19 associates with the spliceosome concomitant with or just after dissociation of U4 small nuclear RNA. Proc. Natl Acad. Sci. USA 90, 10821-10825 (1993).
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 10821-10825
    • Tarn, W.-Y.1    Lee, K.-R.2    Cheng, S.C.3
  • 35
    • 68249149579 scopus 로고    scopus 로고
    • Exon, intron and splice site locations in the spliceosomal B complex
    • Wolf, E. et al. Exon, intron and splice site locations in the spliceosomal B complex. EMBO J. 28, 2283-2292 (2009).
    • (2009) EMBO J. , vol.28 , pp. 2283-2292
    • Wolf, E.1
  • 36
    • 0033612569 scopus 로고    scopus 로고
    • Combined biochemical and electron microscopic analyses reveal the architecture of the mammalian U2 snRNP
    • Krämer, A., Grüter, P., Gröning, K. & Kastner, B. Combined biochemical and electron microscopic analyses reveal the architecture of the mammalian U2 snRNP. J. Cell Biol. 145, 1355-1368 (1999).
    • (1999) J. Cell Biol. , vol.145 , pp. 1355-1368
    • Krämer, A.1    Grüter, P.2    Gröning, K.3    Kastner, B.4
  • 37
    • 0034805909 scopus 로고    scopus 로고
    • Domains in human splicing factors SF3a60 and SF3a66 required for binding to SF3a120, assembly of the 17S U2 snRNP, and prespliceosome formation
    • Nesic, D. & Krämer, A. Domains in human splicing factors SF3a60 and SF3a66 required for binding to SF3a120, assembly of the 17S U2 snRNP, and prespliceosome formation. Mol. Cell. Biol. 21, 6406-6417 (2001).
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6406-6417
    • Nesic, D.1    Krämer, A.2
  • 38
    • 0031976033 scopus 로고    scopus 로고
    • Conservation of structure and subunit interactions in yeast homologues of splicing factor 3b (SF3b) subunits
    • Igel, H., Wells, S., Perriman, R. & Ares, M. Jr. Conservation of structure and subunit interactions in yeast homologues of splicing factor 3b (SF3b) subunits. RNA 4, 1-10 (1998).
    • (1998) RNA , vol.4 , pp. 1-10
    • Igel, H.1    Wells, S.2    Perriman, R.3    Ares, M.4
  • 39
    • 0033999317 scopus 로고    scopus 로고
    • Functional Cus1p is found with Hsh155p in a multiprotein splicing factor associated with U2 snRNA
    • Pauling, M. H., McPheeters, D. S. & Ares, M. Jr. Functional Cus1p is found with Hsh155p in a multiprotein splicing factor associated with U2 snRNA. Mol. Cell. Biol. 20, 2176-2185 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2176-2185
    • Pauling, M.H.1    McPheeters, D.S.2    Ares, M.3
  • 40
    • 33645212088 scopus 로고    scopus 로고
    • U2 snRNA-protein contacts in purified human 17S U2 snRNPs and in spliceosomal A and B complexes
    • Dybkov, O. et al. U2 snRNA-protein contacts in purified human 17S U2 snRNPs and in spliceosomal A and B complexes. Mol. Cell. Biol. 26, 2803-2816 (2006).
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 2803-2816
    • Dybkov, O.1
  • 41
    • 84943545374 scopus 로고    scopus 로고
    • Dynamic contacts of U2, RES, Cwc25, Prp8 and Prp45 proteins with the pre-mRNA branch-site and 3' splice site during catalytic activation and step 1 catalysis in yeast spliceosomes
    • Schneider, C. et al. Dynamic contacts of U2, RES, Cwc25, Prp8 and Prp45 proteins with the pre-mRNA branch-site and 3' splice site during catalytic activation and step 1 catalysis in yeast spliceosomes. PLoS Genet. 11, e1005539 (2015).
    • (2015) PLoS Genet. , vol.11 , pp. e1005539
    • Schneider, C.1
  • 42
    • 0032525135 scopus 로고    scopus 로고
    • Progression through the spliceosome cycle requires Prp38p function for U4/U6 snRNA dissociation
    • Xie, J., Beickman, K., Otte, E. & Rymond, B. C. Progression through the spliceosome cycle requires Prp38p function for U4/U6 snRNA dissociation. EMBO J. 17, 2938-2946 (1998).
    • (1998) EMBO J. , vol.17 , pp. 2938-2946
    • Xie, J.1    Beickman, K.2    Otte, E.3    Rymond, B.C.4
  • 43
    • 0035161567 scopus 로고    scopus 로고
    • Biochemical and genetic analyses of the U5, U6, and U4/U6 x U5 small nuclear ribonucleoproteins from Saccharomyces cerevisiae
    • Stevens, S. W. et al. Biochemical and genetic analyses of the U5, U6, and U4/U6 x U5 small nuclear ribonucleoproteins from Saccharomyces cerevisiae. RNA 7, 1543-1553 (2001).
    • (2001) RNA , vol.7 , pp. 1543-1553
    • Stevens, S.W.1
  • 44
    • 79959407313 scopus 로고    scopus 로고
    • Semiquantitative proteomic analysis of the human spliceosome via a novel two-dimensional gel electrophoresis method
    • Agafonov, D. E. et al. Semiquantitative proteomic analysis of the human spliceosome via a novel two-dimensional gel electrophoresis method. Mol. Cell. Biol. 31, 2667-2682 (2011).
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 2667-2682
    • Agafonov, D.E.1
  • 45
    • 0033575711 scopus 로고    scopus 로고
    • Identification by mass spectrometry and functional analysis of novel proteins of the yeast [U4/U6·U5] tri-snRNP
    • Gottschalk, A. et al. Identification by mass spectrometry and functional analysis of novel proteins of the yeast [U4/U6·U5] tri-snRNP. EMBO J. 18, 4535-4548 (1999).
    • (1999) EMBO J. , vol.18 , pp. 4535-4548
    • Gottschalk, A.1
  • 47
    • 0033047503 scopus 로고    scopus 로고
    • Splicing factor Prp8 governs U4/U6 RNA unwinding during activation of the spliceosome
    • Kuhn, A. N., Li, Z. & Brow, D. A. Splicing factor Prp8 governs U4/U6 RNA unwinding during activation of the spliceosome. Mol. Cell 3, 65-75 (1999).
    • (1999) Mol. Cell , vol.3 , pp. 65-75
    • Kuhn, A.N.1    Li, Z.2    Brow, D.A.3
  • 48
    • 24744465409 scopus 로고    scopus 로고
    • The Prp19-associated complex is required for specifying interactions of U5 and U6 with pre-mRNA during spliceosome activation
    • Chan, S.-P. & Cheng, S.-C. The Prp19-associated complex is required for specifying interactions of U5 and U6 with pre-mRNA during spliceosome activation. J. Biol. Chem. 280, 31190-31199 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 31190-31199
    • Chan, S.-P.1    Cheng, S.-C.2
  • 49
    • 84901929739 scopus 로고    scopus 로고
    • Evidence for a group II intron-like catalytic triplex in the spliceosome
    • Fica, S. M., Mefford, M. A., Piccirilli, J. A. & Staley, J. P. Evidence for a group II intron-like catalytic triplex in the spliceosome. Nat. Struct. Mol. Biol. 21, 464-471 (2014).
    • (2014) Nat. Struct. Mol. Biol. , vol.21 , pp. 464-471
    • Fica, S.M.1    Mefford, M.A.2    Piccirilli, J.A.3    Staley, J.P.4
  • 50
    • 0024280931 scopus 로고
    • Two conserved domains of yeast U2 snRNA are separated by 945 nonessential nucleotides
    • Shuster, E. O. & Guthrie, C. Two conserved domains of yeast U2 snRNA are separated by 945 nonessential nucleotides. Cell 55, 41-48 (1988).
    • (1988) Cell , vol.55 , pp. 41-48
    • Shuster, E.O.1    Guthrie, C.2
  • 51
    • 84938513943 scopus 로고    scopus 로고
    • The architecture of the spliceosomal U4/U6.U5 tri-snRNP
    • Nguyen, T. H. D. et al. The architecture of the spliceosomal U4/U6.U5 tri-snRNP. Nature 523, 47-52 (2015).
    • (2015) Nature , vol.523 , pp. 47-52
    • Nguyen, T.H.D.1
  • 52
    • 0028960809 scopus 로고
    • A novel role for a U5 snRNP protein in 3' splice site selection
    • Umen, J. G. & Guthrie, C. A novel role for a U5 snRNP protein in 3' splice site selection. Genes Dev. 9, 855-868 (1995).
    • (1995) Genes Dev. , vol.9 , pp. 855-868
    • Umen, J.G.1    Guthrie, C.2
  • 53
    • 77957066363 scopus 로고    scopus 로고
    • Preparation of fluorescent pre-mRNA substrates for an smFRET study of pre-mRNA splicing in yeast
    • Abelson, J., Hadjivassiliou, H. & Guthrie, C. Preparation of fluorescent pre-mRNA substrates for an smFRET study of pre-mRNA splicing in yeast. Methods Enzymol. 472, 31-40 (2010).
    • (2010) Methods Enzymol. , vol.472 , pp. 31-40
    • Abelson, J.1    Hadjivassiliou, H.2    Guthrie, C.3
  • 54
    • 0029790609 scopus 로고    scopus 로고
    • A fluorescence-labeling method for sequencing small RNA on polyacrylamide gel
    • Wu, T. P., Ruan, K. C. & Liu, W. Y. A fluorescence-labeling method for sequencing small RNA on polyacrylamide gel. Nucleic Acids Res. 24, 3472-3473 (1996).
    • (1996) Nucleic Acids Res. , vol.24 , pp. 3472-3473
    • Wu, T.P.1    Ruan, K.C.2    Liu, W.Y.3
  • 55
    • 79955631373 scopus 로고    scopus 로고
    • Purification of functional RNA-protein complexes using MS2-MBP
    • Zhou, Z. & Reed, R. Purification of functional RNA-protein complexes using MS2-MBP. Curr. Protoc. Mol. Biol. 63, 27.3.1-27.3.7 (2001).
    • (2001) Curr. Protoc. Mol. Biol. , vol.63 , pp. 2731-2737
    • Zhou, Z.1    Reed, R.2
  • 56
    • 84880848354 scopus 로고    scopus 로고
    • Electron counting and beam-induced motion correction enable nearatomic- resolution single-particle cryo-EM
    • Li, X. et al. Electron counting and beam-induced motion correction enable nearatomic- resolution single-particle cryo-EM. Nat. Methods 10, 584-590 (2013).
    • (2013) Nat. Methods , vol.10 , pp. 584-590
    • Li, X.1
  • 57
    • 84946488108 scopus 로고    scopus 로고
    • CTFFIND4: Fast and accurate defocus estimation from electron micrographs
    • Rohou, A. & Grigorieff, N. CTFFIND4: Fast and accurate defocus estimation from electron micrographs. J. Struct. Biol. 192, 216-221 (2015).
    • (2015) J. Struct. Biol. , vol.192 , pp. 216-221
    • Rohou, A.1    Grigorieff, N.2
  • 58
    • 84868444740 scopus 로고    scopus 로고
    • RELION: Implementation of a Bayesian approach to cryo-EM structure determination
    • Scheres, S. H. RELION: implementation of a Bayesian approach to cryo-EM structure determination. J. Struct. Biol. 180, 519-530 (2012).
    • (2012) J. Struct. Biol. , vol.180 , pp. 519-530
    • Scheres, H.S.1
  • 59
    • 84866078359 scopus 로고    scopus 로고
    • Prevention of overfitting in cryo-EM structure determination
    • Scheres, S. H. W. & Chen, S. Prevention of overfitting in cryo-EM structure determination. Nat. Methods 9, 853-854 (2012).
    • (2012) Nat. Methods , vol.9 , pp. 853-854
    • Scheres, S.H.W.1    Chen, S.2
  • 60
    • 33845332754 scopus 로고    scopus 로고
    • EMAN2: An extensible image processing suite for electron microscopy
    • Tang, G. et al. EMAN2: an extensible image processing suite for electron microscopy. J. Struct. Biol. 157, 38-46 (2007).
    • (2007) J. Struct. Biol. , vol.157 , pp. 38-46
    • Tang, G.1
  • 61
    • 84922727036 scopus 로고    scopus 로고
    • Semi-automated selection of cryo-EM particles in RELION-1.3
    • Scheres, S. H. Semi-automated selection of cryo-EM particles in RELION-1.3. J. Struct. Biol. 189, 114-122 (2015).
    • (2015) J. Struct. Biol. , vol.189 , pp. 114-122
    • Scheres, S.H.1
  • 62
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera-A visualization system for exploratory research and analysis
    • Pettersen, E. F. et al. UCSF Chimera-a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605-1612 (2004).
    • (2004) J. Comput. Chem. , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1
  • 63
    • 84955307962 scopus 로고    scopus 로고
    • Sampling the conformational space of the catalytic subunit of human γ -secretase
    • Bai, X.-C., Rajendra, E., Yang, G., Shi, Y. & Scheres, S. H. W. Sampling the conformational space of the catalytic subunit of human γ -secretase. eLife 4, e11182 (2015).
    • (2015) ELife , vol.4 , pp. e11182
    • Bai, X.-C.1    Rajendra, E.2    Yang, G.3    Shi, Y.4    Scheres, S.H.W.5
  • 64
    • 84894623755 scopus 로고    scopus 로고
    • Quantifying the local resolution of cryo-EM density maps
    • Kucukelbir, A., Sigworth, F. J. & Tagare, H. D. Quantifying the local resolution of cryo-EM density maps. Nat. Methods 11, 63-65 (2014).
    • (2014) Nat. Methods , vol.11 , pp. 63-65
    • Kucukelbir, A.1    Sigworth, F.J.2    Tagare, H.D.3
  • 65
    • 13244281317 scopus 로고    scopus 로고
    • Model-building tools for molecular graphics
    • Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126-2132 (2004).
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Coot, C.K.2
  • 66
    • 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 66, 213-221 (2010).
    • (2010) Acta Crystallogr. D , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 67
    • 84893774907 scopus 로고    scopus 로고
    • Crystal structures of the Lsm complex bound to the 3' end sequence of U6 small nuclear RNA
    • Zhou, L. et al. Crystal structures of the Lsm complex bound to the 3' end sequence of U6 small nuclear RNA. Nature 506, 116-120 (2014).
    • (2014) Nature , vol.506 , pp. 116-120
    • Zhou, L.1
  • 68
    • 79957601559 scopus 로고    scopus 로고
    • Structure of the spliceosomal U4 snRNP core domain and its implication for snRNP biogenesis
    • Leung, A. K. W., Nagai, K. & Li, J. Structure of the spliceosomal U4 snRNP core domain and its implication for snRNP biogenesis. Nature 473, 536-539 (2011).
    • (2011) Nature , vol.473 , pp. 536-539
    • Leung, A.K.W.1    Nagai, K.2    Li, J.3
  • 69
    • 84949215654 scopus 로고    scopus 로고
    • Comparative protein structure modeling using Modeller. Curr. Protoc. Bioinformatics
    • Eswar, N. et al. Comparative protein structure modeling using Modeller. Curr. Protoc. Bioinformatics Chapter 5, 5.6.1-5.6.3 (2014).
    • (2014) Chapter , vol.5 , pp. 561-563
    • Eswar, N.1
  • 70
    • 84860290256 scopus 로고    scopus 로고
    • Conventions and workflows for using Situs
    • Wriggers, W. Conventions and workflows for using Situs. Acta Crystallogr. D 68, 344-351 (2012).
    • (2012) Acta Crystallogr. D , vol.68 , pp. 344-351
    • Wriggers, W.1
  • 71
    • 82055164092 scopus 로고    scopus 로고
    • ViennaRNA package 2.0
    • Lorenz, R. et al. ViennaRNA Package 2.0. Algorithms Mol. Biol. 6, 26 (2011).
    • (2011) Algorithms Mol. Biol. , vol.6 , pp. 26
    • Lorenz, R.1
  • 72
    • 84864953710 scopus 로고    scopus 로고
    • Automated 3D structure composition for large RNAs
    • Popenda, M. et al. Automated 3D structure composition for large RNAs. Nucleic Acids Res. 40, e112 (2012).
    • (2012) Nucleic Acids Res. , vol.40 , pp. e112
    • Popenda, M.1
  • 73
    • 84879797997 scopus 로고    scopus 로고
    • Inhibition of RNA helicase Brr2 by the C-terminal tail of the spliceosomal protein Prp8
    • Mozaffari-Jovin, S. et al. Inhibition of RNA helicase Brr2 by the C-terminal tail of the spliceosomal protein Prp8. Science 341, 80-84 (2013).
    • (2013) Science , vol.341 , pp. 80-84
    • Mozaffari-Jovin, S.1
  • 74
    • 39449114521 scopus 로고    scopus 로고
    • The U1, U2 and U5 snRNAs crosslink to the 5' exon during yeast pre-mRNA splicing
    • McGrail, J. C. & O'Keefe, R. T. The U1, U2 and U5 snRNAs crosslink to the 5' exon during yeast pre-mRNA splicing. Nucleic Acids Res. 36, 814-825 (2008).
    • (2008) Nucleic Acids Res. , vol.36 , pp. 814-825
    • McGrail, J.C.1    O'Keefe, R.T.2
  • 75
    • 84910664664 scopus 로고    scopus 로고
    • Stem-loop 4 of U1 snRNA is essential for splicing and interacts with the U2 snRNP-specific SF3A1 protein during spliceosome assembly
    • Sharma, S., Wongpalee, S. P., Vashisht, A., Wohlschlegel, J. A. & Black, D. L. Stem-loop 4 of U1 snRNA is essential for splicing and interacts with the U2 snRNP-specific SF3A1 protein during spliceosome assembly. Genes Dev. 28, 2518-2531 (2014).
    • (2014) Genes Dev. , vol.28 , pp. 2518-2531
    • Sharma, S.1    Wongpalee, S.P.2    Vashisht, A.3    Wohlschlegel, J.A.4    Black, D.L.5
  • 76
    • 0035053295 scopus 로고    scopus 로고
    • Functional contacts with a range of splicing proteins suggest a central role for Brr2p in the dynamic control of the order of events in spliceosomes of Saccharomyces cerevisiae
    • van Nues, R. W. & Beggs, J. D. Functional contacts with a range of splicing proteins suggest a central role for Brr2p in the dynamic control of the order of events in spliceosomes of Saccharomyces cerevisiae. Genetics 157, 1451-1467 (2001).
    • (2001) Genetics , vol.157 , pp. 1451-1467
    • Van Nues, R.W.1    Beggs, J.D.2


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