메뉴 건너뛰기




Volumn 21, Issue 5, 2014, Pages 464-471

Evidence for a group II intron-like catalytic triplex in the spliceosome

Author keywords

[No Author keywords available]

Indexed keywords

SMALL NUCLEAR RNA;

EID: 84901929739     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.2815     Document Type: Article
Times cited : (90)

References (58)
  • 1
    • 60349104299 scopus 로고    scopus 로고
    • The spliceosome: Design principles of a dynamic RNP machine
    • Wahl, M.C., Will, C.L. & Lührmann, R. The spliceosome: design principles of a dynamic RNP machine. Cell 136, 701-718 (2009).
    • (2009) Cell , vol.136 , pp. 701-718
    • Wahl, M.C.1    Will, C.L.2    Lührmann, R.3
  • 2
    • 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
  • 3
    • 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
  • 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
    • 0022552726 scopus 로고
    • The generality of self-splicing RNA: Relationship to nuclear mRNA splicing
    • Cech, T.R. The generality of self-splicing RNA: relationship to nuclear mRNA splicing. Cell 44, 207-210 (1986).
    • (1986) Cell , vol.44 , pp. 207-210
    • Cech, T.R.1
  • 6
    • 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
  • 7
    • 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
  • 8
    • 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
  • 9
    • 0033166446 scopus 로고    scopus 로고
    • Metal ion catalysis during group II intron self-splicing: Parallels with the spliceosome
    • Sontheimer, E.J., Gordon, P.M. & Piccirilli, J.A. Metal ion catalysis during group II intron self-splicing: parallels with the spliceosome. Genes Dev. 13, 1729-1741 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 1729-1741
    • Sontheimer, E.J.1    Gordon, P.M.2    Piccirilli, J.A.3
  • 10
    • 34250349882 scopus 로고    scopus 로고
    • A second divalent metal ion in the group II intron reaction center
    • Gordon, P.M., Fong, R. & Piccirilli, J.A. A second divalent metal ion in the group II intron reaction center. Chem. Biol. 14, 607-612 (2007).
    • (2007) Chem. Biol. , vol.14 , pp. 607-612
    • Gordon, P.M.1    Fong, R.2    Piccirilli, J.A.3
  • 11
    • 75649116868 scopus 로고    scopus 로고
    • A structural analysis of the group II intron active site and implications for the spliceosome
    • Keating, K.S., Toor, N., Perlman, P.S. & Pyle, A.M. A structural analysis of the group II intron active site and implications for the spliceosome. RNA 16, 1-9 (2010).
    • (2010) RNA , vol.16 , pp. 1-9
    • Keating, K.S.1    Toor, N.2    Perlman, P.S.3    Pyle, A.M.4
  • 12
    • 0033750527 scopus 로고    scopus 로고
    • Deletion of a conserved dinucleotide inhibits the second step of group II intron splicing
    • Mikheeva, S., Murray, H.L., Zhou, H., Turczyk, B.M. & Jarrell, K.A. Deletion of a conserved dinucleotide inhibits the second step of group II intron splicing. RNA 6, 1509-1515 (2000).
    • (2000) RNA , vol.6 , pp. 1509-1515
    • Mikheeva, S.1    Murray, H.L.2    Zhou, H.3    Turczyk, B.M.4    Jarrell, K.A.5
  • 13
    • 38049052541 scopus 로고    scopus 로고
    • Three essential and conserved regions of the group II intron are proximal to the 5′-splice site
    • de Lencastre, A. & Pyle, A.M. Three essential and conserved regions of the group II intron are proximal to the 5′-splice site. RNA 14, 11-24 (2008).
    • (2008) RNA , vol.14 , pp. 11-24
    • De Lencastre, A.1    Pyle, A.M.2
  • 14
    • 0025344901 scopus 로고
    • Base-pairing interactions involving the 5′ and 3′-terminal nucleotides of group II self-splicing introns
    • Jacquier, A. & Michel, F. Base-pairing interactions involving the 5′ and 3′-terminal nucleotides of group II self-splicing introns. J. Mol. Biol. 213, 437-447 (1990).
    • (1990) J. Mol. Biol. , vol.213 , pp. 437-447
    • Jacquier, A.1    Michel, F.2
  • 15
    • 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
  • 16
    • 0028917214 scopus 로고
    • A novel U2-U6 snRNA structure is necessary for mammalian mRNA splicing
    • Sun, J.S. & Manley, J.L. A novel U2-U6 snRNA structure is necessary for mammalian mRNA splicing. Genes Dev. 9, 843-854 (1995).
    • (1995) Genes Dev. , vol.9 , pp. 843-854
    • Sun, J.S.1    Manley, J.L.2
  • 17
    • 67649354912 scopus 로고    scopus 로고
    • Evidence that U2/U6 helix i promotes both catalytic steps of pre-mRNA splicing and rearranges in between these steps
    • Mefford, M.A. & Staley, J.P. Evidence that U2/U6 helix I promotes both catalytic steps of pre-mRNA splicing and rearranges in between these steps. RNA 15, 1386-1397 (2009).
    • (2009) RNA , vol.15 , pp. 1386-1397
    • Mefford, M.A.1    Staley, J.P.2
  • 18
    • 0025001918 scopus 로고
    • Two domains of yeast U6 small nuclear RNA required for both steps of nuclear precursor messenger RNA splicing
    • Fabrizio, P. & Abelson, J.J. Two domains of yeast U6 small nuclear RNA required for both steps of nuclear precursor messenger RNA splicing. Science 250, 404-409 (1990).
    • (1990) Science , vol.250 , pp. 404-409
    • Fabrizio, P.1    Abelson, J.J.2
  • 19
    • 2442661481 scopus 로고    scopus 로고
    • Multiple functions for the invariant AGC triad of U6 snRNA
    • Hilliker, A.K. & Staley, J.P. Multiple functions for the invariant AGC triad of U6 snRNA. RNA 10, 921-928 (2004).
    • (2004) RNA , vol.10 , pp. 921-928
    • Hilliker, A.K.1    Staley, J.P.2
  • 20
    • 0028569768 scopus 로고
    • Catalytic site components common to both splicing steps of a group II intron
    • Chanfreau, G. & Jacquier, A. Catalytic site components common to both splicing steps of a group II intron. Science 266, 1383-1387 (1994).
    • (1994) Science , vol.266 , pp. 1383-1387
    • Chanfreau, G.1    Jacquier, A.2
  • 21
    • 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
  • 22
    • 0027923620 scopus 로고
    • Role of U6 snRNA in 5′ splice site selection
    • Kandels-Lewis, S. & Séraphin, B. Role 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
  • 23
    • 84887115772 scopus 로고    scopus 로고
    • RNA structure analysis of human spliceosomes reveals a compact 3D arrangement of snRNAs at the catalytic core
    • Anokhina, M. et al. RNA structure analysis of human spliceosomes reveals a compact 3D arrangement of snRNAs at the catalytic core. EMBO J. 32, 2804-2818 (2013).
    • (2013) EMBO J. , vol.32 , pp. 2804-2818
    • Anokhina, M.1
  • 25
    • 0023782352 scopus 로고
    • Spliceosomal RNA U6 is remarkably conserved from yeast to mammals
    • Brow, D.A. & Guthrie, C. Spliceosomal RNA U6 is remarkably conserved from yeast to mammals. Nature 334, 213-218 (1988).
    • (1988) Nature , vol.334 , pp. 213-218
    • Brow, D.A.1    Guthrie, C.2
  • 26
    • 44849094904 scopus 로고    scopus 로고
    • Triple-helix structure in telomerase RNA contributes to catalysis
    • Qiao, F. & Cech, T.R. Triple-helix structure in telomerase RNA contributes to catalysis. Nat. Struct. Mol. Biol. 15, 634-640 (2008).
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 634-640
    • Qiao, F.1    Cech, T.R.2
  • 27
    • 78649422018 scopus 로고    scopus 로고
    • A tail recognition by a viral RNA element through assembly of a triple helix
    • Mitton-Fry, R.M., DeGregorio, S.J., Wang, J., Steitz, T.A. & Steitz, J.A. Poly(A) tail recognition by a viral RNA element through assembly of a triple helix. Science 330, 1244-1247 (2010).
    • (2010) Science , vol.330 , pp. 1244-1247
    • Mitton-Fry, R.M.1    Degregorio, S.J.2    Wang, J.3    Steitz, T.A.4    Poly, A.S.J.5
  • 28
    • 84879705616 scopus 로고    scopus 로고
    • Pyrimidine motif triple helix in the Kluyveromyces lactis telomerase RNA pseudoknot is essential for function in vivo
    • Cash, D.D. et al. Pyrimidine motif triple helix in the Kluyveromyces lactis telomerase RNA pseudoknot is essential for function in vivo. Proc. Natl. Acad. Sci. USA 110, 10970-10975 (2013).
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 10970-10975
    • Cash, D.D.1
  • 29
    • 0037102491 scopus 로고    scopus 로고
    • The non-Watson-Crick base pairs and their associated isostericity matrices
    • Leontis, N.B., Stombaugh, J. & Westhof, E. The non-Watson-Crick base pairs and their associated isostericity matrices. Nucleic Acids Res. 30, 3497-3531 (2002).
    • (2002) Nucleic Acids Res. , vol.30 , pp. 3497-3531
    • Leontis, N.B.1    Stombaugh, J.2    Westhof, E.3
  • 30
    • 0028465429 scopus 로고
    • Site-specific RNA crosslinking with 4-thiouridine
    • Sontheimer, E.J. Site-specific RNA crosslinking with 4-thiouridine. Mol. Biol. Rep. 20, 35-44 (1994).
    • (1994) Mol. Biol. Rep. , vol.20 , pp. 35-44
    • Sontheimer, E.J.1
  • 31
    • 3342906885 scopus 로고    scopus 로고
    • New tertiary constraints between the RNA components of active yeast spliceosomes: A photo-crosslinking study
    • Ryan, D.E. et al. New tertiary constraints between the RNA components of active yeast spliceosomes: a photo-crosslinking study. RNA 10, 1251-1265 (2004).
    • (2004) RNA , vol.10 , pp. 1251-1265
    • Ryan, D.E.1
  • 32
    • 0025763145 scopus 로고
    • Crystal structure of Penicillium citrinum P1 nuclease at 2.8 A resolution
    • Volbeda, A., Lahm, A., Sakiyama, F. & Suck, D. Crystal structure of Penicillium citrinum P1 nuclease at 2.8 A resolution. EMBO J. 10, 1607-1618 (1991).
    • (1991) EMBO J. , vol.10 , pp. 1607-1618
    • Volbeda, A.1    Lahm, A.2    Sakiyama, F.3    Suck, D.4
  • 33
    • 0014692862 scopus 로고
    • Structure of transfer RNA: Evidence for interaction between two non-adjacent nucleotide residues in tRNAVal1 from Escherichia coli
    • Yaniv, M., Favre, A. & Barrell, B.G. Structure of transfer RNA: evidence for interaction between two non-adjacent nucleotide residues in tRNAVal1 from Escherichia coli. Nature 223, 1331-1333 (1969).
    • (1969) Nature , vol.223 , pp. 1331-1333
    • Yaniv, M.1    Favre, A.2    Barrell, B.G.3
  • 34
    • 54049155019 scopus 로고    scopus 로고
    • Solution structure of tRNAVal from refinement of homology model against residual dipolar coupling and SAXS data
    • Grishaev, A., Ying, J., Canny, M.D., Pardi, A. & Bax, A. Solution structure of tRNAVal from refinement of homology model against residual dipolar coupling and SAXS data. J. Biomol. NMR 42, 99-109 (2008).
    • (2008) J. Biomol. NMR , vol.42 , pp. 99-109
    • Grishaev, A.1    Ying, J.2    Canny, M.D.3    Pardi, A.4    Bax, A.5
  • 35
    • 0032005336 scopus 로고    scopus 로고
    • Thionucleobases as intrinsic photoaffinity probes of nucleic acid structure and nucleic acid-protein interactions
    • Favre, A., Saintomé, C., Fourrey, J.L., Clivio, P. & Laugâa, P. Thionucleobases as intrinsic photoaffinity probes of nucleic acid structure and nucleic acid-protein interactions. J. Photochem. Photobiol. B 42, 109-124 (1998).
    • (1998) J. Photochem. Photobiol. , vol.42 , pp. 109-124
    • Favre, A.1    Saintomé, C.2    Fourrey, J.L.3    Clivio, P.4    Laugâa, P.5
  • 36
    • 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
  • 37
    • 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
  • 38
    • 0026019713 scopus 로고
    • PRP16 is an RNA-dependent ATPase that interacts transiently with the spliceosome
    • Schwer, B. & Guthrie, C. PRP16 is an RNA-dependent ATPase that interacts transiently with the spliceosome. Nature 349, 494-499 (1991).
    • (1991) Nature , vol.349 , pp. 494-499
    • Schwer, B.1    Guthrie, C.2
  • 39
    • 0036674909 scopus 로고    scopus 로고
    • How Slu7 and Prp18 cooperate in the second step of yeast pre-mRNA splicing
    • James, S.-A., Turner, W. & Schwer, B. How Slu7 and Prp18 cooperate in the second step of yeast pre-mRNA splicing. RNA 8, 1068-1077 (2002).
    • (2002) RNA , vol.8 , pp. 1068-1077
    • James, S.-A.1    Turner, W.2    Schwer, B.3
  • 40
    • 0032055765 scopus 로고    scopus 로고
    • Prp22 a DExH-box RNA helicase, plays two distinct roles in yeast pre-mRNA splicing
    • Schwer, B. & Gross, C.H. Prp22, a DExH-box RNA helicase, plays two distinct roles in yeast pre-mRNA splicing. EMBO J. 17, 2086-2094 (1998).
    • (1998) EMBO J. , vol.17 , pp. 2086-2094
    • Schwer, B.1    Gross, C.H.2
  • 41
    • 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
  • 42
    • 84862865359 scopus 로고    scopus 로고
    • Staying on message: Ensuring fidelity in pre-mRNA splicing
    • Semlow, D.R. & Staley, J.P. Staying on message: ensuring fidelity in pre-mRNA splicing. Trends Biochem. Sci. 37, 263-273 (2012).
    • (2012) Trends Biochem. Sci. , vol.37 , pp. 263-273
    • Semlow, D.R.1    Staley, J.P.2
  • 43
    • 84894228514 scopus 로고    scopus 로고
    • The DExD/H-box ATPase Prp2p destabilizes and proofreads the catalytic RNA core of the spliceosome
    • Wlodaver, A.M. & Staley, J.P. The DExD/H-box ATPase Prp2p destabilizes and proofreads the catalytic RNA core of the spliceosome. RNA 20, 282-294 (2014).
    • (2014) RNA , vol.20 , pp. 282-294
    • Wlodaver, A.M.1    Staley, J.P.2
  • 44
    • 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
  • 45
    • 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
  • 46
    • 0028964998 scopus 로고
    • An RNA tertiary structure of the hepatitis delta agent contains UV-sensitive bases U-712 and U-865 and can form in a bimolecular complex
    • Branch, A.D., Levine, B.J. & Polaskova, J.A. An RNA tertiary structure of the hepatitis delta agent contains UV-sensitive bases U-712 and U-865 and can form in a bimolecular complex. Nucleic Acids Res. 23, 491-499 (1995).
    • (1995) Nucleic Acids Res. , vol.23 , pp. 491-499
    • Branch, A.D.1    Levine, B.J.2    Polaskova, J.A.3
  • 47
    • 0021769550 scopus 로고
    • Stability constants of Mg2+ and Cd2+ complexes of adenine nucleotides and thionucleotides and rate constants for formation and dissociation of MgATP and MgADP
    • Pecoraro, V.L., Hermes, J.D. & Cleland, W.W. Stability constants of Mg2+ and Cd2+ complexes of adenine nucleotides and thionucleotides and rate constants for formation and dissociation of MgATP and MgADP. Biochemistry 23, 5262-5271 (1984).
    • (1984) Biochemistry , vol.23 , pp. 5262-5271
    • Pecoraro, V.L.1    Hermes, J.D.2    Cleland, W.W.3
  • 48
    • 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
  • 49
    • 0024792715 scopus 로고
    • In vitro assembly of yeast U6 snRNP: A functional assay
    • Fabrizio, P., McPheeters, D.S. & Abelson, J. In vitro assembly of yeast U6 snRNP: a functional assay. Genes Dev. 3, 2137-2150 (1989).
    • (1989) Genes Dev. , vol.3 , pp. 2137-2150
    • Fabrizio, P.1    McPheeters, D.S.2    Abelson, J.3
  • 50
    • 0142215475 scopus 로고    scopus 로고
    • Global analysis of protein expression in yeast
    • Ghaemmaghami, S. et al. Global analysis of protein expression in yeast. Nature 425, 737-741 (2003).
    • (2003) Nature , vol.425 , pp. 737-741
    • Ghaemmaghami, S.1
  • 51
    • 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
  • 52
    • 0026090063 scopus 로고
    • In vitro mutagenesis and plasmid shuffling: From cloned gene to mutant yeast
    • Sikorski, R.S. & Boeke, J.D. In vitro mutagenesis and plasmid shuffling: from cloned gene to mutant yeast. Methods Enzymol. 194, 302-318 (1991).
    • (1991) Methods Enzymol. , vol.194 , pp. 302-318
    • Sikorski, R.S.1    Boeke, J.D.2
  • 53
    • 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
  • 54
    • 0037013212 scopus 로고    scopus 로고
    • Characterization of dominant-negative mutants of the DEAH-box splicing factors Prp22 and Prp16
    • Schneider, S., Hotz, H. & Schwer, B. Characterization of dominant-negative mutants of the DEAH-box splicing factors Prp22 and Prp16. J. Biol. Chem. 277, 15452-15458 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 15452-15458
    • Schneider, S.1    Hotz, H.2    Schwer, B.3
  • 55
    • 28544448500 scopus 로고    scopus 로고
    • In vitro selection, characterization, and application of deoxyribozymes that cleave RNA
    • Silverman, S.K. In vitro selection, characterization, and application of deoxyribozymes that cleave RNA. Nucleic Acids Res. 33, 6151-6163 (2005).
    • (2005) Nucleic Acids Res. , vol.33 , pp. 6151-6163
    • Silverman, S.K.1
  • 56
    • 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
  • 58
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.