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Volumn 523, Issue 7558, 2015, Pages 47-52

The architecture of the spliceosomal U4/U6.U5 tri-snRNP

Author keywords

[No Author keywords available]

Indexed keywords

HELICASE; SMALL NUCLEAR RIBONUCLEOPROTEIN; SMALL NUCLEAR RNA; BRR2 PROTEIN, S CEREVISIAE; PRP8 PROTEIN, S CEREVISIAE; RNA HELICASE; SACCHAROMYCES CEREVISIAE PROTEIN; SNU114 PROTEIN, S CEREVISIAE;

EID: 84938513943     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature14548     Document Type: Article
Times cited : (177)

References (75)
  • 2
    • 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
  • 3
    • 70449625597 scopus 로고    scopus 로고
    • Theevolutionarily conserved core design of the catalytic activation step of the yeast spliceosome
    • Fabrizio, P. et al.Theevolutionarily 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
  • 4
    • 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
  • 5
    • 0026605043 scopus 로고
    • U5 snRNA interacts with exon sequences at 59 and 39 splice sites
    • Newman, A. J., Norman, C. U5 snRNA interacts with exon sequences at 59 and 39 splice sites. Cell 68, 743-754 (1992).
    • (1992) Cell , vol.68 , pp. 743-754
    • Newman, A.J.1    Norman, C.2
  • 6
    • 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
  • 7
    • 0035161567 scopus 로고    scopus 로고
    • Biochemical and genetic analyses of the U5,U6, andU4/U6.U5 small nuclear ribonucleoproteins from Saccharomyces cerevisiae
    • Stevens, S.W. et al. Biochemical and genetic analyses of the U5,U6, andU4/U6.U5 small nuclear ribonucleoproteins from Saccharomyces cerevisiae. RNA 7, 1543-1553 (2001).
    • (2001) RNA , vol.7 , pp. 1543-1553
    • Stevens, S.W.1
  • 8
    • 0033575711 scopus 로고    scopus 로고
    • Identification by mass spectrometry and functional analysis of novelproteins of the yeast[U4/U6.U5] tri-snRNP
    • Gottschalk, A. et al. Identification by mass spectrometry and functional analysis of novelproteins of the yeast[U4/U6.U5] tri-snRNP.EMBOJ.18, 4535-4548(1999).
    • (1999) EMBOJ , vol.18 , pp. 4535-4548
    • Gottschalk, A.1
  • 9
    • 33344460290 scopus 로고    scopus 로고
    • Dissection of Prp8 protein defines multiple interactions with crucial RNA sequences in the catalytic core of the spliceosome
    • Turner, I. A., Norman, C. M., Churcher, M. J., Newman, A. J. Dissection of Prp8 protein defines multiple interactions with crucial RNA sequences in the catalytic core of the spliceosome. RNA 12, 375-386 (2006).
    • (2006) RNA , vol.12 , pp. 375-386
    • Turner, I.A.1    Norman, C.M.2    Churcher, M.J.3    Newman, A.J.4
  • 10
    • 84873629024 scopus 로고    scopus 로고
    • Crystal structure of Prp8reveals active site cavity of the spliceosome
    • Galej,W.P.,Oubridge, C.,Newman, A. J.&Nagai,K.Crystal structure of Prp8reveals 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
  • 11
    • 0030976931 scopus 로고    scopus 로고
    • An evolutionarily conserved U5 snRNP-specific protein is a GTP-binding factor closely related to the ribosomal translocase EF-2
    • Fabrizio. P., Laggerbauer, B., Lauber, J., Lane, W. S., Luhrmann, R. An evolutionarily conserved U5 snRNP-specific protein is a GTP-binding factor closely related to the ribosomal translocase EF-2.EMBO J. 16, 4092-4106 (1997).
    • (1997) EMBO J. , vol.16 , pp. 4092-4106
    • Fabrizio, P.1    Laggerbauer, B.2    Lauber, J.3    Lane, W.S.4    Luhrmann, R.5
  • 12
    • 33746441457 scopus 로고    scopus 로고
    • The EF-G-like GTPase Snu114p regulates spliceosome dynamics mediated by Brr2p, a DExD/H box ATPase
    • Small, E. C., Leggett, S. R., Winans, A. A., Staley, J. P. The EF-G-like GTPase Snu114p regulates spliceosome dynamics mediated by Brr2p, a DExD/H box ATPase. Mol. Cell 23, 389-399 (2006).
    • (2006) Mol. Cell , vol.23 , pp. 389-399
    • Small, E.C.1    Leggett, S.R.2    Winans, A.A.3    Staley, J.P.4
  • 13
    • 0041344523 scopus 로고    scopus 로고
    • Mutagenesis suggests several roles of Snu114p in pre-mRNAsplicing
    • Bartels. C., Urlaub, H., Luhrmann, R., Fabrizio P. Mutagenesis suggests several roles of Snu114p in pre-mRNAsplicing. J. Biol. Chem. 278, 28324-28334 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 28324-28334
    • Bartels, C.1    Urlaub, H.2    Luhrmann, R.3    Fabrizio, P.4
  • 14
    • 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
  • 15
    • 0032515969 scopus 로고    scopus 로고
    • The human U5-200kD DEXH-box protein unwinds U4/U6 RNA duplices in vitro
    • Laggerbauer, B., Achsel, T., Lu hrmann, 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    Luhrmann, R.3
  • 16
    • 33745613530 scopus 로고    scopus 로고
    • The network of protein-protein interactions within the human U4/U6.U5 tri-snRNP
    • Liu, S., Rauhut, R., Vornlocher, H. P., Luhrmann, R. The network of protein-protein interactions within the human U4/U6.U5 tri-snRNP. RNA 12, 1418-1430 (2006).
    • (2006) RNA , vol.12 , pp. 1418-1430
    • Liu, S.1    Rauhut, R.2    Vornlocher, H.P.3    Luhrmann, R.4
  • 17
    • 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
  • 18
    • 33749672830 scopus 로고    scopus 로고
    • Organization of core spliceosomal components U5 snRNA loop i and U4/U6 Di-snRNP within U4/U6.U5 Tri-snRNP as revealed by electron cryomicroscopy
    • Sander, B. et al. Organization of core spliceosomal components U5 snRNA loop I and U4/U6 Di-snRNP within U4/U6.U5 Tri-snRNP as revealed by electron cryomicroscopy. Mol. Cell 24, 267-278 (2006).
    • (2006) Mol. Cell , vol.24 , pp. 267-278
    • Sander, B.1
  • 19
    • 55549142496 scopus 로고    scopus 로고
    • Localization of Prp8, Brr2, Snu114 and U4/U6 proteins in the yeast tri-snRNPby electron microscopy
    • Hacker, I. et al. Localization of Prp8, Brr2, Snu114 and U4/U6 proteins in the yeast tri-snRNPby electron microscopy. Nature Struct.Mol. Biol. 15, 1206-1212 (2008).
    • (2008) Nature Struct.Mol. Biol. , vol.15 , pp. 1206-1212
    • Hacker, I.1
  • 20
    • 67650538546 scopus 로고    scopus 로고
    • Experimental observation of the improvement in MTF from backthinning a CMOS direct electron detector
    • McMullan, G. et al. Experimental observation of the improvement in MTF from backthinning a CMOS direct electron detector. Ultramicroscopy 109, 1144-1147 (2009).
    • (2009) Ultramicroscopy , vol.109 , pp. 1144-1147
    • McMullan, G.1
  • 21
    • 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. Nature Methods 10, 584-590 (2013).
    • (2013) Nature Methods , vol.10 , pp. 584-590
    • Li, X.1
  • 22
    • 84855818650 scopus 로고    scopus 로고
    • A Bayesian view on cryo-EM structure determination
    • Scheres, S. H. A Bayesian view on cryo-EM structure determination. J. Mol. Biol. 415, 406-418 (2012).
    • (2012) J. Mol. Biol. , vol.415 , pp. 406-418
    • Scheres, S.H.1
  • 23
    • 84923368907 scopus 로고    scopus 로고
    • How cryo-EM is revolutionizing structural biology
    • Bai, X. C., McMullan, G., Scheres, S. H. How cryo-EM is revolutionizing structural biology. Trends Biochem. Sci. 40, 49-57 (2015).
    • (2015) Trends Biochem. Sci. , vol.40 , pp. 49-57
    • Bai, X.C.1    McMullan, G.2    Scheres, S.H.3
  • 24
    • 84920942671 scopus 로고    scopus 로고
    • Beam-induced motion correction for sub-megadalton cryo-EM particles
    • Scheres, S. H. Beam-induced motion correction for sub-megadalton cryo-EM particles. Elife 3, e03665 (2014).
    • (2014) Elife , vol.3 , pp. e03665
    • Scheres, S.H.1
  • 25
    • 84866078359 scopus 로고    scopus 로고
    • Prevention of overfitting in cryo-EM structure determination
    • Scheres, S. H., Chen, S. Prevention of overfitting in cryo-EM structure determination. Nature Methods 9, 853-854 (2012).
    • (2012) Nature Methods , vol.9 , pp. 853-854
    • Scheres, S.H.1    Chen, S.2
  • 26
    • 0242516080 scopus 로고    scopus 로고
    • Two crystal structures demonstrate large conformational changes in the eukaryotic ribosomal translocase
    • Jørgensen, R. et al. Two crystal structures demonstrate large conformational changes in the eukaryotic ribosomal translocase. Nature Struct. Biol. 10, 379-385 (2003).
    • (2003) Nature Struct. Biol. , vol.10 , pp. 379-385
    • Jørgensen, R.1
  • 27
    • 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
  • 28
    • 0032406465 scopus 로고    scopus 로고
    • Protein-RNA interactions in the U5 snRNP of Saccharomyces cerevisiae
    • Dix, I., Russell, C. S., O'Keefe, R. T., Newman, A. J., Beggs, J. D. Protein-RNA interactions in the U5 snRNP of Saccharomyces cerevisiae. RNA 4, 1675-1686 (1998).
    • (1998) RNA , vol.4 , pp. 1675-1686
    • Dix, I.1    Russell, C.S.2    O'Keefe, R.T.3    Newman, A.J.4    Beggs, J.D.5
  • 29
    • 0033607476 scopus 로고    scopus 로고
    • Identification characterization and crystal structure analysis of the human spliceosomal U5 snRNP-specific 15 kD protein
    • Reuter, K., Nottrott, S., Fabrizio, P., Luhrmann, R., Ficner, R. Identification, characterization and crystal structure analysis of the human spliceosomal U5 snRNP-specific 15 kD protein. J. Mol. Biol. 294, 515-525 (1999).
    • (1999) J. Mol. Biol. , vol.294 , pp. 515-525
    • Reuter, K.1    Nottrott, S.2    Fabrizio, P.3    Luhrmann, R.4    Ficner, R.5
  • 30
    • 58149231008 scopus 로고    scopus 로고
    • ATP-dependent unwinding of U4/U6 snRNAs by the Brr2 helicase requires the C terminus of Prp8
    • Maeder, C., Kutach, A. K., Guthrie, C. ATP-dependent unwinding of U4/U6 snRNAs by the Brr2 helicase requires the C terminus of Prp8. Nature Struct. Mol. Biol. 16, 42-48 (2009).
    • (2009) Nature Struct. Mol. Biol. , vol.16 , pp. 42-48
    • Maeder, C.1    Kutach, A.K.2    Guthrie, C.3
  • 31
    • 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
  • 32
    • 84879797997 scopus 로고    scopus 로고
    • Inhibition ofRNA helicaseBrr2 by the C-terminal tail of the spliceosomal protein Prp8
    • Mozaffari-Jovin, S. et al. Inhibition ofRNA helicaseBrr2 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
  • 33
    • 34147095881 scopus 로고    scopus 로고
    • Binding of the human Prp31 Nop domain to a composite RNA-protein platform in U4 snRNP
    • Liu, S. et al. Binding of the human Prp31 Nop domain to a composite RNA-protein platform in U4 snRNP. Science 316, 115-120 (2007).
    • (2007) Science , vol.316 , pp. 115-120
    • Liu, S.1
  • 34
    • 33748778456 scopus 로고    scopus 로고
    • RNA structural requirements for the association of the spliceosomal hPrp31 protein with the U4 and U4atac small nuclear ribonucleoproteins
    • Schultz, A., Nottrott, S., Hartmuth, K., Luhrmann, R. RNA structural requirements for the association of the spliceosomal hPrp31 protein with the U4 and U4atac small nuclear ribonucleoproteins. J. Biol. Chem. 281, 28278-28286 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 28278-28286
    • Schultz, A.1    Nottrott, S.2    Hartmuth, K.3    Luhrmann, R.4
  • 35
    • 0032484029 scopus 로고    scopus 로고
    • Functional and structural characterization of the Prp3 binding domain of the yeast Prp4 splicing factor
    • Ayadi, L. et al. Functional and structural characterization of the Prp3 binding domain of the yeast Prp4 splicing factor. J. Mol. Biol. 284, 673-687 (1998).
    • (1998) J. Mol. Biol. , vol.284 , pp. 673-687
    • Ayadi, L.1
  • 36
    • 84867308898 scopus 로고    scopus 로고
    • Structural bioinformatics of the human spliceosomal proteome
    • Korneta, I., Magnus, M., Bujnicki, J. M. Structural bioinformatics of the human spliceosomal proteome. Nucleic Acids Res. 40, 7046-7065 (2012).
    • (2012) Nucleic Acids Res , vol.40 , pp. 7046-7065
    • Korneta, I.1    Magnus, M.2    Bujnicki, J.M.3
  • 37
    • 0037107418 scopus 로고    scopus 로고
    • Hierarchical clustered protein interactions with U4/U6 snRNA: A biochemical role for U4/U6 proteins
    • Nottrott, S., Urlaub, H., Luhrmann, R. Hierarchical, clustered protein interactions with U4/U6 snRNA: a biochemical role for U4/U6 proteins. EMBO J. 21, 5527-5538 (2002).
    • (2002) EMBO J. , vol.21 , pp. 5527-5538
    • Nottrott, S.1    Urlaub, H.2    Luhrmann, R.3
  • 38
    • 0027238743 scopus 로고
    • The biochemical defects of prp4-1 and prp6-1 yeast splicingmutants reveal that the PRP6 protein is required for the accumulation of the [U4/U6.U5] tri-snRNP
    • Galisson, F., Legrain, P. The biochemical defects of prp4-1 and prp6-1 yeast splicingmutants reveal that the PRP6 protein is required for the accumulation of the [U4/U6.U5] tri-snRNP. Nucleic Acids Res. 21, 1555-1562 (1993).
    • (1993) Nucleic Acids Res , vol.21 , pp. 1555-1562
    • Galisson, F.1    Legrain, P.2
  • 39
    • 0034640124 scopus 로고    scopus 로고
    • The human homologue of the yeast splicing factor prp6p contains multiple TPR elements and is stably associated with the U5 snRNP via protein-protein interactions
    • Makarov, E. M., Makarova, O. V., Achsel, T., Luhrmann, R. The human homologue of the yeast splicing factor prp6p contains multiple TPR elements and is stably associated with the U5 snRNP via protein-protein interactions. J. Mol. Biol. 298, 567-575 (2000).
    • (2000) J. Mol. Biol. , vol.298 , pp. 567-575
    • Makarov, E.M.1    Makarova, O.V.2    Achsel, T.3    Luhrmann, R.4
  • 40
    • 35848950003 scopus 로고    scopus 로고
    • Prp8 mutations that cause human retinitis pigmentosa lead to a U5 snRNP maturation defect in yeast
    • Boon, K. L. et al. Prp8 mutations that cause human retinitis pigmentosa lead to a U5 snRNP maturation defect in yeast. Nature Struct. Mol. Biol. 14, 1077-1083 (2007).
    • (2007) Nature Struct. Mol. Biol. , vol.14 , pp. 1077-1083
    • Boon, K.L.1
  • 41
    • 84868583242 scopus 로고    scopus 로고
    • The Prp8 RNase H-like domain inhibits Brr2-mediated U4/U6 snRNAunwinding by blockingBrr2loading onto theU4 snRNA
    • Mozaffari-Jovin, S. et al. The Prp8 RNase H-like domain inhibits Brr2-mediated U4/U6 snRNAunwinding by blockingBrr2loading onto theU4 snRNA. GenesDev. 26, 2422-2434 (2012).
    • (2012) Genes Dev , vol.26 , pp. 2422-2434
    • Mozaffari-Jovin, S.1
  • 42
    • 84868592766 scopus 로고    scopus 로고
    • Brr2p-mediated conformational rearrangements in the spliceosomeduring activation and substrate repositioning
    • Hahn, D., Kudla, G., Tollervey, D., Beggs, J. D. Brr2p-mediated conformational rearrangements in the spliceosomeduring activation and substrate repositioning. Genes Dev. 26, 2408-2421 (2012).
    • (2012) Genes Dev , vol.26 , pp. 2408-2421
    • Hahn, D.1    Kudla, G.2    Tollervey, D.3    Beggs, J.D.4
  • 43
    • 34447132375 scopus 로고    scopus 로고
    • Structural basis for DNA duplex separation by a superfamily-2 helicase
    • Buttner K., Nehring, S., Hofner, K. P. Structural basis for DNA duplex separation by a superfamily-2 helicase. Nature Struct. Mol. Biol. 14, 647-652 (2007).
    • (2007) Nature Struct. Mol. Biol. , vol.14 , pp. 647-652
    • Buttner, K.1    Nehring, S.2    Hofner, K.P.3
  • 44
    • 84879663355 scopus 로고    scopus 로고
    • Elongation factorG bound to the ribosome in an intermediate state of translocation
    • Tourigny, D. S., Fernández, I. S., Kelley, A. C.&Ramakrishnan, V. Elongation factorG bound to the ribosome in an intermediate state of translocation. Science 340, 1235490 (2013).
    • (2013) Science , vol.340 , pp. 1235490
    • Tourigny, D.S.1    Fernández, I.S.2    Kelley, A.C.3    Ramakrishnan, V.4
  • 45
    • 84920987347 scopus 로고    scopus 로고
    • Conformational changes of elongationfactorGonthe ribosomeduring tRNAtranslocation
    • Lin. J., Gagnon, M. G., Bulkley, D., Steitz, T. A. Conformational changes of elongationfactorGonthe ribosomeduring tRNAtranslocation. Cell160,219-227 (2015).
    • (2015) Cell , vol.160 , pp. 219-227
    • Lin, J.1    Gagnon, M.G.2    Bulkley, D.3    Steitz, T.A.4
  • 46
    • 0033900068 scopus 로고    scopus 로고
    • Suppressors of a cold-sensitivemutation in yeast U4RNA define five domains in the splicing factor Prp8 that influence spliceosome activation
    • Kuhn, A. N., Brow, D. A. Suppressors of a cold-sensitivemutation in yeast U4RNA define five domains in the splicing factor Prp8 that influence spliceosome activation. Genetics 155, 1667-1682 (2000).
    • (2000) Genetics , vol.155 , pp. 1667-1682
    • Kuhn, A.N.1    Brow, D.A.2
  • 47
    • 0029958501 scopus 로고    scopus 로고
    • A spontaneous duplication in U6 spliceosomal RNA uncouples the early and late functions of the ACAGAelement in vivo
    • Li, Z., Brow, D. A. A spontaneous duplication in U6 spliceosomal RNA uncouples the early and late functions of the ACAGAelement in vivo. RNA 2, 879-894 (1996).
    • (1996) RNA , vol.2 , pp. 879-894
    • Li, Z.1    Brow, D.A.2
  • 48
    • 41749109563 scopus 로고    scopus 로고
    • Crystal structure of a self-spliced group II intron
    • Toor, N., Keating, K. S., Taylor, S. D., Pyle, A. M. Crystal structure of a self-spliced group II intron. Science 320, 77-82 (2008).
    • (2008) Science , vol.320 , pp. 77-82
    • Toor, N.1    Keating, K.S.2    Taylor, S.D.3    Pyle, A.M.4
  • 50
    • 0026261876 scopus 로고
    • Five easy pieces
    • Sharp, P. A. Five easy pieces. Science 254, 663 (1991).
    • (1991) Science , vol.254 , pp. 663
    • Sharp, P.A.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. Nature Struct. Mol. Biol. 21, 175-179 (2014).
    • (2014) Nature Struct. Mol. Biol. , vol.21 , pp. 175-179
    • Schreieck, A.1
  • 52
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determinationof local defocus and specimen tilt in electron microscopy
    • Mindell, J.A.&Grigorieff, N. Accurate determinationof local defocus and specimen tilt in electron microscopy. J. Struct. Biol. 142, 334-347 (2003).
    • (2003) J. Struct. Biol. , vol.142 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 53
    • 84881432897 scopus 로고    scopus 로고
    • PRIME: Probabilistic initial 3D model generation for single-particle cryo-electron microscopy
    • Elmlund, H., Elmlund, D., Bengio, S. PRIME: probabilistic initial 3D model generation for single-particle cryo-electron microscopy. Structure 21, 1299-1306 (2013).
    • (2013) Structure , vol.21 , pp. 1299-1306
    • Elmlund, H.1    Elmlund, D.2    Bengio, S.3
  • 54
    • 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. Nature Methods 11, 63-65 (2014).
    • (2014) Nature Methods , vol.11 , pp. 63-65
    • Kucukelbir, A.1    Sigworth, F.J.2    Tagare, H.D.3
  • 55
    • 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
  • 57
    • 33845332754 scopus 로고    scopus 로고
    • EMAN2: An extensive image processing suite for electron microscopy
    • Tang, G. et al. EMAN2: an extensive 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
  • 58
    • 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
  • 60
    • 39449115394 scopus 로고    scopus 로고
    • I-TASSER server for protein 3D structure prediction
    • Zhang, Y. I-TASSER server for protein 3D structure prediction. BMC Bioinformatics 9, 40 (2008).
    • (2008) BMC Bioinformatics , vol.9 , pp. 40
    • Zhang, Y.1
  • 61
    • 34247362408 scopus 로고    scopus 로고
    • Superfamily assignments for the yeast proteome through integration of structure prediction with the gene ontology
    • Malmstrom, L. et al. Superfamily assignments for the yeast proteome through integration of structure prediction with the gene ontology. PLoS Biol. 5, e76 (2007).
    • (2007) PLoS Biol. , vol.5 , pp. e76
    • Malmstrom, L.1
  • 62
    • 78649513584 scopus 로고    scopus 로고
    • The effect of ASP-His-Ser/Thr-Trp tetrad on the thermostability of WD40-repeat proteins
    • Wu, X. H.,Chen, R. C.,Gao, Y.&Wu, Y.D. The effect of Asp-His-Ser/Thr-Trp tetrad on the thermostability of WD40-repeat proteins. Biochemistry 49, 10237-10245 (2010).
    • (2010) Biochemistry , vol.49 , pp. 10237-10245
    • Wu, X.H.1    Chen, R.C.2    Gao, Y.3    Wu, Y.D.4
  • 63
    • 80051921913 scopus 로고    scopus 로고
    • ModeRNA server: An online tool for modeling RNA 3D structures
    • Rother, M. et al. ModeRNA server: an online tool for modeling RNA 3D structures. Bioinformatics 27, 2441-2442 (2011).
    • (2011) Bioinformatics , vol.27 , pp. 2441-2442
    • Rother, M.1
  • 64
    • 34447579888 scopus 로고    scopus 로고
    • Analysis of pre-mRNAand pre-rRNA processing factor Snu13p structure and mutants
    • Dobbyn, H. C. et al. Analysis of pre-mRNAand pre-rRNA processing factor Snu13p structure and mutants. Biochem. Biophys. Res. Commun. 360, 857-862 (2007).
    • (2007) Biochem. Biophys. Res. Commun. , vol.360 , pp. 857-862
    • Dobbyn, H.C.1
  • 65
    • 79957601559 scopus 로고    scopus 로고
    • Structure of the spliceosomal U4snRNP core domain and its implication for snRNP biogenesis
    • Leung, A. K., Nagai, K., Li, J. Structure of the spliceosomal U4snRNP core domain and its implication for snRNP biogenesis. Nature 473, 536-539 (2011).
    • (2011) Nature , vol.473 , pp. 536-539
    • Leung, A.K.1    Nagai, K.2    Li, J.3
  • 66
    • 0030859441 scopus 로고    scopus 로고
    • Alternative 39-end processing of U5 snRNA by RNase III
    • Chanfreau, G., Elela, S. A., Ares, M. Jr & Guthrie, C. Alternative 39-end processing of U5 snRNA by RNase III. Genes Dev. 11, 2741-2751 (1997).
    • (1997) Genes Dev. , vol.11 , pp. 2741-2751
    • Chanfreau, G.1    Elela, S.A.2    Ares, M.3    Guthrie, C.4
  • 67
    • 84893774907 scopus 로고    scopus 로고
    • Crystal structures of the Lsmcomplex bound to the 39end sequence of U6 small nuclear RNA
    • Zhou, L. et al. Crystal structures of the Lsmcomplex bound to the 39end sequence of U6 small nuclear RNA. Nature 506, 116-120 (2014).
    • (2014) Nature , vol.506 , pp. 116-120
    • Zhou, L.1
  • 68
    • 2342522014 scopus 로고    scopus 로고
    • Suppression of multiple substrate mutations by spliceosomal prp8 alleles suggests functional correlations with ribosomal ambiguity mutants
    • Query, C. C., Konarska, M. M. Suppression of multiple substrate mutations by spliceosomal prp8 alleles suggests functional correlations with ribosomal ambiguity mutants. Mol. Cell 14, 343-354 (2004).
    • (2004) Mol. Cell , vol.14 , pp. 343-354
    • Query, C.C.1    Konarska, M.M.2
  • 69
    • 0030030194 scopus 로고    scopus 로고
    • Mutagenesis of the yeast gene PRP8 reveals domains governing the specificity and fidelity of 39 splice site selection
    • Umen, J. G., Guthrie, C. Mutagenesis of the yeast gene PRP8 reveals domains governing the specificity and fidelity of 39 splice site selection. Genetics 143, 723-739 (1996).
    • (1996) Genetics , vol.143 , pp. 723-739
    • Umen, J.G.1    Guthrie, C.2
  • 70
    • 34249890532 scopus 로고    scopus 로고
    • Opposing classes of prp8 allelesmodulate the transition between the catalytic steps of pre-mRNA splicing
    • Liu, L., Query, C. C.&Konarska,M.M.Opposing classes of prp8 allelesmodulate the transition between the catalytic steps of pre-mRNA splicing. Nature Struct. Mol. Biol. 14, 519-526 (2007).
    • (2007) Nature Struct. Mol. Biol. , vol.14 , pp. 519-526
    • Liu, L.1    Query, C.C.2    Konarska, M.M.3
  • 71
    • 0034852411 scopus 로고    scopus 로고
    • Evidence for a role of Sky1p-mediated phosphorylation in 39 splice site recognition involving bothPrp8 and Prp17/Slu4
    • Dagher, S. F., Fu, X. D. Evidence for a role of Sky1p-mediated phosphorylation in 39 splice site recognition involving bothPrp8 and Prp17/Slu4.RNA 7, 1284-1297 (2001).
    • (2001) RNA , vol.7 , pp. 1284-1297
    • Dagher, S.F.1    Fu, X.D.2
  • 72
    • 0033966187 scopus 로고    scopus 로고
    • Extensive genetic interactions between PRP8 and PRP17/CDC40, two yeast genes involved in pre-mRNA splicing and cell cycle progression
    • Ben-Yehuda, S. et al. Extensive genetic interactions between PRP8 and PRP17/CDC40, two yeast genes involved in pre-mRNA splicing and cell cycle progression. Genetics 154, 61-71 (2000).
    • (2000) Genetics , vol.154 , pp. 61-71
    • Ben-Yehuda, S.1
  • 73
    • 0033179776 scopus 로고    scopus 로고
    • Allele-specific genetic interactions between Prp8 and RNA active site residues suggest a function for Prp8 at the catalytic core of the spliceosome
    • Collins, C. A., Guthrie, C. Allele-specific genetic interactions between Prp8 and RNA active site residues suggest a function for Prp8 at the catalytic core of the spliceosome. Genes Dev. 13, 1970-1982 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 1970-1982
    • Collins, C.A.1    Guthrie, C.2
  • 74
    • 0033179750 scopus 로고    scopus 로고
    • Functional interactions of Prp8 with both splice sites at the spliceosomal catalytic center
    • Siatecka, M., Reyes, J. L., Konarska, M. M. Functional interactions of Prp8 with both splice sites at the spliceosomal catalytic center. Genes Dev. 13, 1983-1993 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 1983-1993
    • Siatecka, M.1    Reyes, J.L.2    Konarska, M.M.3
  • 75
    • 0033047503 scopus 로고    scopus 로고
    • Splicing factor Prp8 governsU4/U6 RNA unwinding during activation of the spliceosome
    • Kuhn, A. N., Li, Z.&Brow, D. A. Splicing factor Prp8 governsU4/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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.