메뉴 건너뛰기




Volumn 537, Issue 7619, 2016, Pages 197-201

Cryo-EM structure of the spliceosome immediately after branching

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE; FUNGAL RNA; MAGNESIUM; MESSENGER RNA PRECURSOR; NUCLEOTIDE; NUCLEOTIDE G; PRP16 HELICASE; PRP8 REVERSE TRANSCRIPTASE; RIBOZYME; RNA DIRECTED DNA POLYMERASE; RNA HELICASE; SMALL NUCLEAR RNA; UNCLASSIFIED DRUG; ADENOSINE TRIPHOSPHATASE; CWC25 PROTEIN, S CEREVISIAE; NUCLEAR PROTEIN; PRP16 PROTEIN, S CEREVISIAE; PRP8 PROTEIN, S CEREVISIAE; RNA PRECURSOR; RNA SPLICING; RNA SPLICING FACTOR; SACCHAROMYCES CEREVISIAE PROTEIN; SMALL NUCLEAR RIBONUCLEOPROTEIN; U2 SMALL NUCLEAR RNA; U5 SMALL NUCLEAR RNA; U6 SMALL NUCLEAR RNA; YJU2 PROTEIN, S CEREVISIAE;

EID: 84986612633     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature19316     Document Type: Article
Times cited : (183)

References (84)
  • 2
    • 0001468848 scopus 로고    scopus 로고
    • (eds Gesteland, R. F., Cech, T. R., Atkins, J. F) (Cold Spring Harbor Laboratory Press
    • Burge, C. B., Tuschl, T., Sharp, P. A. in The RNA World II (eds Gesteland, R. F., Cech, T. R., Atkins, J. F.) 525-560 (Cold Spring Harbor Laboratory Press, 1999).
    • (1999) The RNA World II , pp. 525-560
    • Burge, C.B.1    Tuschl, T.2    Sharp, P.A.3
  • 4
    • 0141924550 scopus 로고    scopus 로고
    • The Prp19p-associated complex in spliceosome activation
    • Chan, S.-P., Kao, D.-I., Tsai, W.-Y., Cheng, S.-C. The Prp19p-associated complex in spliceosome activation. Science 302, 279-282 (2003).
    • (2003) Science , vol.302 , pp. 279-282
    • Chan, S.-P.1    Kao, D.-I.2    Tsai, W.-Y.3    Cheng, S.-C.4
  • 5
    • 0036269649 scopus 로고    scopus 로고
    • Characterization of interactions among the Cef1p-Prp19p-associated splicing complex
    • Ohi, M. D., Gould, K. L. Characterization of interactions among the Cef1p-Prp19p-associated splicing complex. RNA 8, 798-815 (2002).
    • (2002) RNA , vol.8 , pp. 798-815
    • Ohi, M.D.1    Gould, K.L.2
  • 6
    • 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
  • 7
    • 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
  • 8
    • 0027923620 scopus 로고
    • Involvement of U6 snRNA in 5 splice site selection
    • Kandels-Lewis, S., Séraphin, B. Involvement of U6 snRNA in 5 splice site selection. Science 262, 2035-2039 (1993).
    • (1993) Science , vol.262 , pp. 2035-2039
    • Kandels-Lewis, S.1    Séraphin, B.2
  • 9
    • 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
  • 10
    • 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
  • 11
    • 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
  • 12
    • 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
  • 13
    • 84879311174 scopus 로고    scopus 로고
    • Molecular dissection of step 2 catalysis of yeast pre-mRNA splicing investigated in a purified system
    • Ohrt, T.et al. Molecular dissection of step 2 catalysis of yeast pre-mRNA splicing investigated in a purified system. RNA 19, 902-915 (2013).
    • (2013) RNA , vol.19 , pp. 902-915
    • Ohrt, T.1
  • 14
    • 84861984263 scopus 로고    scopus 로고
    • Structure function and regulation of spliceosomal RNA helicases
    • Cordin, O., Hahn, D., Beggs, J. D. Structure, function and regulation of spliceosomal RNA helicases. Curr. Opin. Cell Biol. 24, 431-438 (2012).
    • (2012) Curr. Opin. Cell Biol. , vol.24 , pp. 431-438
    • Cordin, O.1    Hahn, D.2    Beggs, J.D.3
  • 15
    • 44949117567 scopus 로고    scopus 로고
    • A conformational rearrangement in the spliceosome sets the stage for Prp22-dependent mRNA release
    • Schwer, B. A conformational rearrangement in the spliceosome sets the stage for Prp22-dependent mRNA release. Mol. Cell 30, 743-754 (2008).
    • (2008) Mol. Cell , vol.30 , pp. 743-754
    • Schwer, B.1
  • 16
    • 0026088747 scopus 로고
    • Requirement of the RNA helicase-like protein PRP22 for release of messenger RNA from spliceosomes
    • Company, M., Arenas, J., Abelson, J. Requirement of the RNA helicase-like protein PRP22 for release of messenger RNA from spliceosomes. Nature 349, 487-493 (1991).
    • (1991) Nature , vol.349 , pp. 487-493
    • Company, M.1    Arenas, J.2    Abelson, J.3
  • 17
    • 29144515824 scopus 로고    scopus 로고
    • Spliceosome disassembly catalyzed by Prp43 and its associated components Ntr1 and Ntr2
    • Tsai, R.-T. et al. Spliceosome disassembly catalyzed by Prp43 and its associated components Ntr1 and Ntr2. Genes Dev. 19, 2991-3003 (2005).
    • (2005) Genes Dev. , vol.19 , pp. 2991-3003
    • Tsai, R.-T.1
  • 18
    • 77950516144 scopus 로고    scopus 로고
    • Conformational dynamics of single pre-mRNA molecules during in vitro splicing
    • Abelson, J. et al. Conformational dynamics of single pre-mRNA molecules during in vitro splicing. Nat. Struct. Mol. Biol. 17, 504-512 (2010).
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 504-512
    • Abelson, J.1
  • 19
    • 84958967476 scopus 로고    scopus 로고
    • Cryo-EM structure of the yeast U4/U6.U5 tri-snRNP at 3.7 A resolution
    • Nguyen, T. H. D. et al. Cryo-EM structure of the yeast U4/U6.U5 tri-snRNP at 3.7 A resolution. Nature 530, 298-302 (2016).
    • (2016) Nature , vol.530 , pp. 298-302
    • Nguyen, T.H.D.1
  • 20
    • 84956686435 scopus 로고    scopus 로고
    • The 3.8 A structure of the U4/U6.U5 tri-snRNP: Insights into spliceosome assembly and catalysis
    • Wan, R. et al. The 3.8 A 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
  • 21
    • 84873629024 scopus 로고    scopus 로고
    • Crystal structure of Prp8 reveals active site cavity of the spliceosome
    • Galej, W. P., Oubridge, C., Newman, A. J., Nagai, K. Crystal structure of Prp8 reveals active site cavity of the spliceosome. Nature 493, 638-643 (2013).
    • (2013) Nature , vol.493 , pp. 638-643
    • Galej, W.P.1    Oubridge, C.2    Newman, A.J.3    Nagai, K.4
  • 22
    • 84858799296 scopus 로고    scopus 로고
    • Cwc2 and its human homologue RBM22 promote an active conformation of the spliceosome catalytic centre
    • Rasche, N. et al. Cwc2 and its human homologue RBM22 promote an active conformation of the spliceosome catalytic centre. EMBO J. 31, 1591-1604 (2012).
    • (2012) EMBO J. , vol.31 , pp. 1591-1604
    • Rasche, N.1
  • 23
    • 34147179830 scopus 로고    scopus 로고
    • U2 toggles iteratively between the stem IIa and stem IIc conformations to promote pre-mRNA splicing
    • Hilliker, A. K., Mefford, M. A., Staley, J. P. U2 toggles iteratively between the stem IIa and stem IIc conformations to promote pre-mRNA splicing. Genes Dev. 21, 821-834 (2007).
    • (2007) Genes Dev. , vol.21 , pp. 821-834
    • Hilliker, A.K.1    Mefford, M.A.2    Staley, J.P.3
  • 24
    • 34147174235 scopus 로고    scopus 로고
    • Rearrangement of competing U2 RNA helices within the spliceosome promotes multiple steps in splicing
    • Perriman, R. J., Ares, M., Jr. Rearrangement of competing U2 RNA helices within the spliceosome promotes multiple steps in splicing. Genes Dev. 21, 811-820 (2007).
    • (2007) Genes Dev. , vol.21 , pp. 811-820
    • Perriman, R.J.1    Ares, M.2
  • 25
    • 73249134403 scopus 로고    scopus 로고
    • Physical and genetic interactions of yeast Cwc21p, an ortholog of human SRm300/SRRM2, suggest a role at the catalytic center of the spliceosome
    • Grainger, R. J., Barrass, J. D., Jacquier, A., Rain, J.-C., Beggs, J. D. Physical and genetic interactions of yeast Cwc21p, an ortholog of human SRm300/SRRM2, suggest a role at the catalytic center of the spliceosome. RNA 15, 2161-2173 (2009).
    • (2009) RNA , vol.15 , pp. 2161-2173
    • Grainger, R.J.1    Barrass, J.D.2    Jacquier, A.3    Rain, J.-C.4    Beggs, J.D.5
  • 26
    • 84942474131 scopus 로고    scopus 로고
    • Structure of a yeast spliceosome at 3.6-angstrom resolution
    • Yan, C. et al. Structure of a yeast spliceosome at 3.6-angstrom resolution. Science 349, 1182-1191 (2015).
    • (2015) Science , vol.349 , pp. 1182-1191
    • Yan, C.1
  • 27
    • 84878849387 scopus 로고    scopus 로고
    • Structural basis of Brr2-Prp8 interactions and implications for U5 snRNP biogenesis and the spliceosome active site
    • Nguyen, T. H. D. et al. Structural basis of Brr2-Prp8 interactions and implications for U5 snRNP biogenesis and the spliceosome active site. Structure 21, 910-919 (2013).
    • (2013) Structure , vol.21 , pp. 910-919
    • Nguyen, T.H.D.1
  • 28
    • 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
  • 29
    • 44949246374 scopus 로고    scopus 로고
    • Nought may endure but mutability": Spliceosome dynamics and the regulation of splicing
    • Smith, D. J., Query, C. C., Konarska, M. M. "Nought may endure but mutability": spliceosome dynamics and the regulation of splicing. Mol. Cell 30, 657-666 (2008).
    • (2008) Mol. Cell , vol.30 , pp. 657-666
    • Smith, D.J.1    Query, C.C.2    Konarska, M.M.3
  • 30
    • 32444443532 scopus 로고    scopus 로고
    • Repositioning of the reaction intermediate within the catalytic center of the spliceosome
    • Konarska, M. M., Vilardell, J., Query, C. C. Repositioning of the reaction intermediate within the catalytic center of the spliceosome. Mol. Cell 21, 543-553 (2006).
    • (2006) Mol. Cell , vol.21 , pp. 543-553
    • Konarska, M.M.1    Vilardell, J.2    Query, C.C.3
  • 31
    • 0002690513 scopus 로고    scopus 로고
    • Site-specific crosslinks of yeast U6 snRNA to the pre-mRNA near the 5 splice site
    • Kim, C. H., Abelson, J. Site-specific crosslinks of yeast U6 snRNA to the pre-mRNA near the 5 splice site. RNA 2, 995-1010 (1996).
    • (1996) RNA , vol.2 , pp. 995-1010
    • Kim, C.H.1    Abelson, J.2
  • 32
    • 84888357821 scopus 로고    scopus 로고
    • Crystal structure of the human eIF4AIII-CWC22 complex shows how a DEAD-box protein is inhibited by a MIF4G domain
    • Buchwald, G., Schüssler, S., Basquin, C., Le Hir, H., Conti, E. Crystal structure of the human eIF4AIII-CWC22 complex shows how a DEAD-box protein is inhibited by a MIF4G domain. Proc. Natl Acad. Sci. USA 110, E4611-E4618 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. E4611-E4618
    • Buchwald, G.1    Schüssler, S.2    Basquin, C.3    Le Hir, H.4    Conti, E.5
  • 33
    • 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
  • 34
    • 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
  • 35
    • 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
  • 36
    • 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
  • 37
    • 84908347683 scopus 로고    scopus 로고
    • Crystal structure of a eukaryotic group II intron lariat
    • Robart, A. R., Chan, R. T., Peters, J. K., Rajashankar, K. R., Toor, N. Crystal structure of a eukaryotic group II intron lariat. Nature 514, 193-197 (2014).
    • (2014) Nature , vol.514 , pp. 193-197
    • Robart, A.R.1    Chan, R.T.2    Peters, J.K.3    Rajashankar, K.R.4    Toor, N.5
  • 38
    • 84873041707 scopus 로고    scopus 로고
    • Link of NTR-mediated spliceosome disassembly with DEAH-box ATPases Prp2, Prp16, and Prp22
    • Chen, H.-C., Tseng, C.-K., Tsai, R.-T., Chung, C.-S., Cheng, S.-C. Link of NTR-mediated spliceosome disassembly with DEAH-box ATPases Prp2, Prp16, and Prp22. Mol. Cell. Biol. 33, 514-525 (2013).
    • (2013) Mol. Cell. Biol. , vol.33 , pp. 514-525
    • Chen, H.-C.1    Tseng, C.-K.2    Tsai, R.-T.3    Chung, C.-S.4    Cheng, S.-C.5
  • 39
    • 71449119694 scopus 로고    scopus 로고
    • Reconstitution of both steps of Saccharomyces cerevisiae splicing with purified spliceosomal components
    • Warkocki, Z. et al. Reconstitution of both steps of Saccharomyces cerevisiae splicing with purified spliceosomal components. Nat. Struct. Mol. Biol. 16, 1237-1243 (2009).
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 1237-1243
    • Warkocki, Z.1
  • 40
    • 70350532246 scopus 로고    scopus 로고
    • Cwc25 is a novel splicing factor required after Prp2 and Yju2 to facilitate the first catalytic reaction
    • Chiu, Y.-F. et al. Cwc25 is a novel splicing factor required after Prp2 and Yju2 to facilitate the first catalytic reaction. Mol. Cell. Biol. 29, 5671-5678 (2009).
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 5671-5678
    • Chiu, Y.-F.1
  • 41
    • 84890208734 scopus 로고    scopus 로고
    • Biased Brownian ratcheting leads to pre-mRNA remodeling and capture prior to first-step splicing
    • Krishnan, R. et al. Biased Brownian ratcheting leads to pre-mRNA remodeling and capture prior to first-step splicing. Nat. Struct. Mol. Biol. 20, 1450-1457 (2013).
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 1450-1457
    • Krishnan, R.1
  • 42
    • 66149157000 scopus 로고    scopus 로고
    • Insights into substrate stabilization from snapshots of the peptidyl transferase center of the intact 70S ribosome
    • Voorhees, R. M., Weixlbaumer, A., Loakes, D., Kelley, A. C., Ramakrishnan, V. Insights into substrate stabilization from snapshots of the peptidyl transferase center of the intact 70S ribosome. Nat. Struct. Mol. Biol. 16, 528-533 (2009).
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 528-533
    • Voorhees, R.M.1    Weixlbaumer, A.2    Loakes, D.3    Kelley, A.C.4    Ramakrishnan, V.5
  • 43
    • 84959420989 scopus 로고    scopus 로고
    • Spliceosomal DEAH-Box ATPases remodel pre-mRNA to activate alternative splice sites
    • Semlow, D. R., Blanco, M. R., Walter, N. G., Staley, J. P. Spliceosomal DEAH-Box ATPases remodel pre-mRNA to activate alternative splice sites. Cell 164, 985-998 (2016).
    • (2016) Cell , vol.164 , pp. 985-998
    • Semlow, D.R.1    Blanco, M.R.2    Walter, N.G.3    Staley, J.P.4
  • 44
    • 78650446117 scopus 로고    scopus 로고
    • DEAH-box ATPase Prp16 has dual roles in remodeling of the spliceosome in catalytic steps
    • Tseng, C.-K., Liu, H.-L., Cheng, S.-C. DEAH-box ATPase Prp16 has dual roles in remodeling of the spliceosome in catalytic steps. RNA 17, 145-154 (2011).
    • (2011) RNA , vol.17 , pp. 145-154
    • Tseng, C.-K.1    Liu, H.-L.2    Cheng, S.-C.3
  • 45
    • 0027065506 scopus 로고
    • A conformational rearrangement in the spliceosome is dependent on PRP16 and ATP hydrolysis
    • Schwer, B., Guthrie, C. A conformational rearrangement in the spliceosome is dependent on PRP16 and ATP hydrolysis. EMBO J. 11, 5033-5039 (1992).
    • (1992) EMBO J. , vol.11 , pp. 5033-5039
    • Schwer, B.1    Guthrie, C.2
  • 46
    • 23944469448 scopus 로고    scopus 로고
    • The Isy1p component of the NineTeen complex interacts with the ATPase Prp16p to regulate the fidelity of pre-mRNA splicing
    • Villa, T., Guthrie, C. The Isy1p component of the NineTeen complex interacts with the ATPase Prp16p to regulate the fidelity of pre-mRNA splicing. Genes Dev. 19, 1894-1904 (2005).
    • (2005) Genes Dev. , vol.19 , pp. 1894-1904
    • Villa, T.1    Guthrie, C.2
  • 47
    • 0029349060 scopus 로고
    • Prp16p, Slu7p, and Prp8p interact with the 3 splice site in two distinct stages during the second catalytic step of pre-mRNA splicing
    • Umen, J. G., Guthrie, C. Prp16p, Slu7p, and Prp8p interact with the 3 splice site in two distinct stages during the second catalytic step of pre-mRNA splicing. RNA 1, 584-597 (1995).
    • (1995) RNA , vol.1 , pp. 584-597
    • Umen, J.G.1    Guthrie, C.2
  • 48
    • 84894250615 scopus 로고    scopus 로고
    • Endogenous U2•U5•U6 snRNA complexes in S. Pombe are intron lariat spliceosomes
    • Chen, W. et al. Endogenous U2•U5•U6 snRNA complexes in S. pombe are intron lariat spliceosomes. RNA 20, 308-320 (2014).
    • (2014) RNA , vol.20 , pp. 308-320
    • Chen, W.1
  • 49
    • 84954550544 scopus 로고    scopus 로고
    • CryoEM structures of two spliceosomal complexes: Starter and dessert at the spliceosome feast
    • Nguyen, T. H. D. et al. CryoEM structures of two spliceosomal complexes: starter and dessert at the spliceosome feast. Curr. Opin. Struct. Biol. 36, 48-57 (2016).
    • (2016) Curr. Opin. Struct. Biol. , vol.36 , pp. 48-57
    • Nguyen, T.H.D.1
  • 50
    • 84904513583 scopus 로고    scopus 로고
    • A homolog of lariat-debranching enzyme modulates turnover of branched RNA
    • Garrey, S. M. et al. A homolog of lariat-debranching enzyme modulates turnover of branched RNA. RNA 20, 1337-1348 (2014).
    • (2014) RNA , vol.20 , pp. 1337-1348
    • Garrey, S.M.1
  • 51
    • 84893810594 scopus 로고    scopus 로고
    • RNA polymerase II termination involves C-terminal-domain tyrosine dephosphorylation by CPF subunit Glc7
    • Schreieck, A. et al. RNA polymerase II termination involves C-terminal-domain tyrosine dephosphorylation by CPF subunit Glc7. Nat. Struct. Mol. Biol. 21, 175-179 (2014).
    • (2014) Nat. Struct. Mol. Biol. , vol.21 , pp. 175-179
    • Schreieck, A.1
  • 53
    • 0037068447 scopus 로고    scopus 로고
    • Comprehensive proteomic analysis of the human spliceosome
    • Zhou, Z., Licklider, L. J., Gygi, S. P., Reed, R. Comprehensive proteomic analysis of the human spliceosome. Nature 419, 182-185 (2002).
    • (2002) Nature , vol.419 , pp. 182-185
    • Zhou, Z.1    Licklider, L.J.2    Gygi, S.P.3    Reed, R.4
  • 54
    • 84954467080 scopus 로고    scopus 로고
    • Assembly and dynamics of the U4/U6 di-snRNP by single-molecule FRET
    • Hardin, J. W., Warnasooriya, C., Kondo, Y., Nagai, K., Rueda, D. Assembly and dynamics of the U4/U6 di-snRNP by single-molecule FRET. Nucleic Acids Res. 43, 10963-10974 (2015).
    • (2015) Nucleic Acids Res. , vol.43 , pp. 10963-10974
    • Hardin, J.W.1    Warnasooriya, C.2    Kondo, Y.3    Nagai, K.4    Rueda, D.5
  • 55
    • 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
  • 56
    • 84880848354 scopus 로고    scopus 로고
    • Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM
    • Li, X. et al. Electron counting and beam-induced motion correction enable near-atomic-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. W. 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, S.H.W.1
  • 59
    • 84922727036 scopus 로고    scopus 로고
    • Semi-automated selection of cryo-EM particles in RELION-1.3
    • Scheres, S. H. W. 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.W.1
  • 60
    • 84955307962 scopus 로고    scopus 로고
    • Sampling the conformational space of the catalytic subunit of human-secretase
    • Bai, X.-C., Rajendra, E., Yang, G., Shi, Y., Scheres, S. H. W. Sampling the conformational space of the catalytic subunit of human-secretase. eLife 4, 1485 (2015).
    • (2015) ELife , vol.4 , pp. 1485
    • Bai, X.-C.1    Rajendra, E.2    Yang, G.3    Shi, Y.4    Scheres, S.H.W.5
  • 61
    • 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
  • 62
    • 84880607763 scopus 로고    scopus 로고
    • High-resolution noise substitution to measure overfitting and validate resolution in 3D structure determination by single particle electron cryomicroscopy
    • Chen, S. et al. High-resolution noise substitution to measure overfitting and validate resolution in 3D structure determination by single particle electron cryomicroscopy. Ultramicroscopy 135, 24-35 (2013).
    • (2013) Ultramicroscopy , vol.135 , pp. 24-35
    • Chen, S.1
  • 63
    • 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
  • 64
    • 84555189176 scopus 로고    scopus 로고
    • Structure of the mRNA splicing complex component Cwc2: Insights into RNA recognition
    • Lu, P. et al. Structure of the mRNA splicing complex component Cwc2: insights into RNA recognition. Biochem. J. 441, 591-597 (2012).
    • (2012) Biochem. J. , vol.441 , pp. 591-597
    • Lu, P.1
  • 65
    • 84923886545 scopus 로고    scopus 로고
    • 113Cd NMR experiments reveal an unusual metal cluster in the solution structure of the yeast splicing protein Bud31p
    • van Roon, A.-M. M. et al. 113Cd NMR experiments reveal an unusual metal cluster in the solution structure of the yeast splicing protein Bud31p. Angew. Chem. Int. Edn Engl. 54, 4861-4864 (2015).
    • (2015) Angew. Chem. Int. Edn Engl. , vol.54 , pp. 4861-4864
    • Van Roon, A.-M.M.1
  • 66
    • 84904815625 scopus 로고    scopus 로고
    • SWISS-MODEL: Modelling protein tertiary and quaternary structure using evolutionary information
    • Biasini, M. et al. SWISS-MODEL: modelling protein tertiary and quaternary structure using evolutionary information. Nucleic Acids Res. 42, W252-W258 (2014).
    • (2014) Nucleic Acids Res. , vol.42 , pp. W252-W258
    • Biasini, M.1
  • 67
    • 0043123216 scopus 로고    scopus 로고
    • GeneSilico protein structure prediction meta-server
    • Kurowski, M. A., Bujnicki, J. M. GeneSilico protein structure prediction meta-server. Nucleic Acids Res. 31, 3305-3307 (2003).
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3305-3307
    • Kurowski, M.A.1    Bujnicki, J.M.2
  • 68
    • 0032514483 scopus 로고    scopus 로고
    • Crystal structure of the spliceosomal U2B"-U2A protein complex bound to a fragment of U2 small nuclear RNA
    • Price, S. R., Evans, P. R., Nagai, K. Crystal structure of the spliceosomal U2B"-U2A protein complex bound to a fragment of U2 small nuclear RNA. Nature 394, 645-650 (1998).
    • (1998) Nature , vol.394 , pp. 645-650
    • Price, S.R.1    Evans, P.R.2    Nagai, K.3
  • 69
    • 79959946169 scopus 로고    scopus 로고
    • Cross-linking ligation, and sequencing of hybrids reveals RNA-RNA interactions in yeast
    • Kudla, G., Granneman, S., Hahn, D., Beggs, J. D., Tollervey, D. Cross-linking, ligation, and sequencing of hybrids reveals RNA-RNA interactions in yeast. Proc. Natl Acad. Sci. USA 108, 10010-10015 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 10010-10015
    • Kudla, G.1    Granneman, S.2    Hahn, D.3    Beggs, J.D.4    Tollervey, D.5
  • 70
    • 84925156346 scopus 로고    scopus 로고
    • The I-TASSER Suite: Protein structure and function prediction
    • Yang, J. et al. The I-TASSER Suite: protein structure and function prediction. Nat. Methods 12, 7-8 (2015).
    • (2015) Nat. Methods , vol.12 , pp. 7-8
    • Yang, J.1
  • 71
    • 77954958169 scopus 로고    scopus 로고
    • Prp43p contains a processive helicase structural architecture with a specific regulatory domain
    • Walbott, H. et al. Prp43p contains a processive helicase structural architecture with a specific regulatory domain. EMBO J. 29, 2194-2204 (2010).
    • (2010) EMBO J. , vol.29 , pp. 2194-2204
    • Walbott, H.1
  • 74
    • 84921777915 scopus 로고    scopus 로고
    • Tools for macromolecular model building and refinement into electron cryo-microscopy reconstructions
    • Brown, A. et al. Tools for macromolecular model building and refinement into electron cryo-microscopy reconstructions. Acta Crystallogr. D Biol. Crystallogr. 71, 136-153 (2015).
    • (2015) Acta Crystallogr. D Biol. Crystallogr. , vol.71 , pp. 136-153
    • Brown, A.1
  • 75
    • 33845345287 scopus 로고    scopus 로고
    • Visualizing density maps with UCSF Chimera
    • Goddard, T. D., Huang, C. C., Ferrin, T. E. Visualizing density maps with UCSF Chimera. J. Struct. Biol. 157, 281-287 (2007).
    • (2007) J. Struct. Biol. , vol.157 , pp. 281-287
    • Goddard, T.D.1    Huang, C.C.2    Ferrin, T.E.3
  • 76
    • 84868035651 scopus 로고    scopus 로고
    • Visualizing group II intron catalysis through the stages of splicing
    • Marcia, M., Pyle, A. M. Visualizing group II intron catalysis through the stages of splicing. Cell 151, 497-507 (2012).
    • (2012) Cell , vol.151 , pp. 497-507
    • Marcia, M.1    Pyle, A.M.2
  • 77
    • 84952638804 scopus 로고    scopus 로고
    • The exon junction complex as a node of post-transcriptional networks
    • Le Hir, H., Sauliere, J., Wang, Z. The exon junction complex as a node of post-transcriptional networks. Nat. Rev. Mol. Cell Biol. 17, 41-54 (2016).
    • (2016) Nat. Rev. Mol. Cell Biol. , vol.17 , pp. 41-54
    • Le Hir, H.1    Sauliere, J.2    Wang, Z.3
  • 78
    • 42249093677 scopus 로고    scopus 로고
    • Isolation of an active step i spliceosome and composition of its RNP core
    • Bessonov, S., Anokhina, M., Will, C. L., Urlaub, H., Lührmann, R. Isolation of an active step I spliceosome and composition of its RNP core. Nature 452, 846-850 (2008).
    • (2008) Nature , vol.452 , pp. 846-850
    • Bessonov, S.1    Anokhina, M.2    Will, C.L.3    Urlaub, H.4    Lührmann, R.5
  • 79
    • 84871825274 scopus 로고    scopus 로고
    • Human spliceosomal protein CWC22 plays a role in coupling splicing to exon junction complex deposition and nonsense-mediated decay
    • Alexandrov, A., Colognori, D., Shu, M.-D., Steitz, J. A. Human spliceosomal protein CWC22 plays a role in coupling splicing to exon junction complex deposition and nonsense-mediated decay. Proc. Natl Acad. Sci. USA 109, 21313-21318 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 21313-21318
    • Alexandrov, A.1    Colognori, D.2    Shu, M.-D.3    Steitz, J.A.4
  • 80
    • 84866916889 scopus 로고    scopus 로고
    • CWC22 connects pre-mRNA splicing and exon junction complex assembly
    • Steckelberg, A.-L., Boehm, V., Gromadzka, A. M., Gehring, N. H. CWC22 connects pre-mRNA splicing and exon junction complex assembly. Cell Reports 2, 454-461 (2012).
    • (2012) Cell Reports , vol.2 , pp. 454-461
    • Steckelberg, A.-L.1    Boehm, V.2    Gromadzka, A.M.3    Gehring, N.H.4
  • 81
    • 84867232894 scopus 로고    scopus 로고
    • Human CWC22 escorts the helicase eIF4AIII to spliceosomes and promotes exon junction complex assembly
    • Barbosa, I. et al. Human CWC22 escorts the helicase eIF4AIII to spliceosomes and promotes exon junction complex assembly. Nat. Struct. Mol. Biol. 19, 983-990 (2012).
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 983-990
    • Barbosa, I.1
  • 82
    • 33747182255 scopus 로고    scopus 로고
    • The crystal structure of the exon junction complex reveals how it maintains a stable grip on mRNA
    • Bono, F., Ebert, J., Lorentzen, E., Conti, E. The crystal structure of the exon junction complex reveals how it maintains a stable grip on mRNA. Cell 126, 713-725 (2006).
    • (2006) Cell , vol.126 , pp. 713-725
    • Bono, F.1    Ebert, J.2    Lorentzen, E.3    Conti, E.4
  • 83
    • 33749332762 scopus 로고    scopus 로고
    • Structure of the exon junction core complex with a trapped DEAD-box ATPase bound to RNA
    • Ersen, C. B. F. et al. Structure of the exon junction core complex with a trapped DEAD-box ATPase bound to RNA. Science 313, 1968-1972 (2006).
    • (2006) Science , vol.313 , pp. 1968-1972
    • Ersen, C.B.F.1
  • 84
    • 3242886389 scopus 로고    scopus 로고
    • MOLPROBITY: Structure validation and all-atom contact analysis for nucleic acids and their complexes
    • Davis, I. W., Murray, L. W., Richardson, J. S., Richardson, D. C. MOLPROBITY: structure validation and all-atom contact analysis for nucleic acids and their complexes. Nucleic Acids Res. 32, W615-W619 (2004).
    • (2004) Nucleic Acids Res. , vol.32 , pp. W615-W619
    • Davis, I.W.1    Murray, L.W.2    Richardson, J.S.3    Richardson, D.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.