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Volumn 16, Issue 12, 2009, Pages 1237-1243

Reconstitution of both steps of Saccharomyces cerevisiae splicing with purified spliceosomal components

Author keywords

[No Author keywords available]

Indexed keywords

RIBONUCLEOPROTEIN; RIBONUCLEOPROTEIN PRP16; RIBONUCLEOPROTEIN SLU7; RNA HELICASE; RNA HELICASE CWC25; RNA HELICASE PRP18; RNA HELICASE PRP2; RNA HELICASE SPP2; UNCLASSIFIED DRUG;

EID: 71449119694     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.1729     Document Type: Article
Times cited : (141)

References (43)
  • 1
    • 0003604405 scopus 로고    scopus 로고
    • (eds. Gesteland, R.F., Cech, T.R. & Atkins, J.F.) Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • Will, C.L. & Lührmann, R. Spliceosome structure and function. in RNA World (eds. Gesteland, R.F., Cech, T.R. & Atkins, J.F.) 369-400 (Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, 2006).
    • (2006) Spliceosome Structure and Function in RNA World , pp. 369-400
    • Will, C.L.1    Lührmann, R.2
  • 2
    • 0032489021 scopus 로고    scopus 로고
    • Mechanical devices of the spliceosome: Motors, clocks, springs, and things
    • Staley, J.P. & Guthrie, C. Mechanical devices of the spliceosome: motors, clocks, springs, and things. Cell 92, 315-326 (1998).
    • (1998) Cell , vol.92 , pp. 315-326
    • Staley, J.P.1    Guthrie, C.2
  • 4
    • 0344198459 scopus 로고    scopus 로고
    • The spliceosome: The most complex macromolecular machine in the cell?
    • Nilsen, T.W. The spliceosome: the most complex macromolecular machine in the cell? Bioessays 25, 1147-1149 (2003).
    • (2003) Bioessays , vol.25 , pp. 1147-1149
    • Nilsen, T.W.1
  • 5
    • 48249113056 scopus 로고    scopus 로고
    • Translocation and unwinding mechanisms of RNA and DNA helicases
    • Pyle, A.M. Translocation and unwinding mechanisms of RNA and DNA helicases. Annu. Rev. Biophys. 37, 317-336 (2008).
    • (2008) Annu. Rev. Biophys , vol.37 , pp. 317-336
    • Pyle, A.M.1
  • 6
    • 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
  • 7
    • 0028158655 scopus 로고
    • The splicing factor PRP2, a putative RNA helicase, interacts directly with pre-mRNA
    • Teigelkamp, S., McGarvey, M., Plumpton, M. & Beggs, J.D. The splicing factor PRP2, a putative RNA helicase, interacts directly with pre-mRNA. EMBO J. 13, 888-897 (1994).
    • (1994) EMBO J , vol.13 , pp. 888-897
    • Teigelkamp, S.1    McGarvey, M.2    Plumpton, M.3    Beggs, J.D.4
  • 8
    • 0025064910 scopus 로고
    • Interactions of PRP2 protein with pre-mRNA splicing complexes in Saccharomyces cerevisiae
    • King, D.S. & Beggs, J.D. Interactions of PRP2 protein with pre-mRNA splicing complexes in Saccharomyces cerevisiae. Nucleic Acids Res. 18, 6559-6564 (1990).
    • (1990) Nucleic Acids Res , vol.18 , pp. 6559-6564
    • King, D.S.1    Beggs, J.D.2
  • 9
    • 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
  • 10
    • 0029965552 scopus 로고    scopus 로고
    • Spliceosome activation by PRP2 ATPase prior to the frst transesterifcation reaction of pre-mRNA splicing
    • Kim, S.H. & Lin, R.J. Spliceosome activation by PRP2 ATPase prior to the frst transesterifcation reaction of pre-mRNA splicing. Mol. Cell. Biol. 16, 6810-6819 (1996).
    • (1996) Mol. Cell. Biol , vol.16 , pp. 6810-6819
    • Kim, S.H.1    Lin, R.J.2
  • 11
    • 70449625597 scopus 로고    scopus 로고
    • The evolutionarily conserved core design of the catalytic activation step of the yeast spliceosome
    • in the press
    • Fabrizio, P. et al. The evolutionarily conserved core design of the catalytic activation step of the yeast spliceosome. Mol. Cell (in the press).
    • Mol. Cell
    • Fabrizio, P.1
  • 12
    • 0027287852 scopus 로고
    • A mechanism to enhance mRNA splicing fdelity: The RNA-dependent ATPase Prp16 governs usage of a discard pathway for aberrant lariat intermediates
    • Burgess, S.M. & Guthrie, C. A mechanism to enhance mRNA splicing fdelity: the RNA-dependent ATPase Prp16 governs usage of a discard pathway for aberrant lariat intermediates. Cell 73, 1377-1391 (1993).
    • (1993) Cell , vol.73 , pp. 1377-1391
    • Burgess, S.M.1    Guthrie, C.2
  • 13
    • 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
  • 14
    • 0025117752 scopus 로고
    • PRP18, a protein required for the second reaction in pre-mRNA splicing
    • Vijayraghavan, U. & Abelson, J. PRP18, a protein required for the second reaction in pre-mRNA splicing. Mol. Cell. Biol. 10, 324-332 (1990).
    • (1990) Mol. Cell. Biol , vol.10 , pp. 324-332
    • Vijayraghavan, U.1    Abelson, J.2
  • 15
    • 0027404721 scopus 로고
    • Stages in the second reaction of pre-mRNA splicing: The final step is ATP independent
    • Horowitz, D.S. & Abelson, J. Stages in the second reaction of pre-mRNA splicing: the fnal step is ATP independent. Genes Dev. 7, 320-329 (1993). (Pubitemid 23084407)
    • (1993) Genes and Development , vol.7 , Issue.2 , pp. 320-329
    • Horowitz, D.S.1    Abelson, J.2
  • 16
    • 0029397324 scopus 로고
    • The second catalytic step of pre-mRNA splicing
    • Umen, J.G. & Guthrie, C. The second catalytic step of pre-mRNA splicing. RNA 1, 869-885 (1995).
    • (1995) RNA , vol.1 , pp. 869-885
    • Umen, J.G.1    Guthrie, C.2
  • 17
    • 0029146556 scopus 로고
    • SLU7 and a novel activity, SSF1, act during the PRP16-dependent step of yeast pre-mRNA splicing
    • Ansari, A. & Schwer, B. SLU7 and a novel activity, SSF1, act during the PRP16-dependent step of yeast pre-mRNA splicing. EMBO J. 14, 4001-4009 (1995).
    • (1995) EMBO J , vol.14 , pp. 4001-4009
    • Ansari, A.1    Schwer, B.2
  • 18
    • 0029949595 scopus 로고    scopus 로고
    • Requirement for SLU7 in yeast pre-mRNA splicing is dictated by the distance between the branchpoint and the 3′ splice site
    • Brys, A. & Schwer, B. Requirement for SLU7 in yeast pre-mRNA splicing is dictated by the distance between the branchpoint and the 3′ splice site. RNA 2, 707-717 (1996).
    • (1996) RNA , vol.2 , pp. 707-717
    • Brys, A.1    Schwer, B.2
  • 19
    • 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
  • 20
    • 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
  • 21
    • 46449086933 scopus 로고    scopus 로고
    • Both catalytic steps of nuclear pre-mRNA splicing are reversible
    • Tseng, C.K. & Cheng, S.C. Both catalytic steps of nuclear pre-mRNA splicing are reversible. Science 320, 1782-1784 (2008).
    • (2008) Science , vol.320 , pp. 1782-1784
    • Tseng, C.K.1    Cheng, S.C.2
  • 22
    • 33745860086 scopus 로고    scopus 로고
    • Protein composition and electron microscopy structure of affnity-purifed human spliceosomal B complexes isolated under physiological conditions
    • Deckert, J. et al. Protein composition and electron microscopy structure of affnity-purifed 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
  • 23
    • 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
  • 24
    • 0037073946 scopus 로고    scopus 로고
    • Small nuclear ribonucleoprotein remodeling during catalytic activation of the spliceosome
    • Makarov, E.M. et al. Small nuclear ribonucleoprotein remodeling during catalytic activation of the spliceosome. Science 298, 2205-2208 (2002).
    • (2002) Science , vol.298 , pp. 2205-2208
    • Makarov, E.M.1
  • 25
    • 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
  • 26
    • 0029312195 scopus 로고
    • The fnal stages of spliceosome maturation require Spp2p that can interact with the DEAH box protein Prp2p and promote step 1 of splicing
    • Roy, J., Kim, K., Maddock, J.R., Anthony, J.G. & Woolford, J.L. Jr. The fnal stages of spliceosome maturation require Spp2p that can interact with the DEAH box protein Prp2p and promote step 1 of splicing. RNA 1, 375-390 (1995).
    • (1995) RNA , vol.1 , pp. 375-390
    • Roy, J.1    Kim, K.2    Maddock, J.R.3    Anthony, J.G.4    Woolford Jr., J.L.5
  • 27
    • 34547155595 scopus 로고    scopus 로고
    • A novel splicing factor, Yju2, is associated with NTC and acts after Prp2 in promoting the frst catalytic reaction of pre-mRNA splicing
    • Liu, Y.C., Chen, H.C., Wu, N.Y. & Cheng, S.C. A novel splicing factor, Yju2, is associated with NTC and acts after Prp2 in promoting the frst catalytic reaction of pre-mRNA splicing. Mol. Cell. Biol. 27, 5403-5413 (2007).
    • (2007) Mol. Cell. Biol , vol.27 , pp. 5403-5413
    • Liu, Y.C.1    Chen, H.C.2    Wu, N.Y.3    Cheng, S.C.4
  • 28
    • 58949099708 scopus 로고    scopus 로고
    • The splicing factor Prp17 interacts with the U2, U5 and U6 SnRNPs and associates with the spliceosome pre-and post-catalysis
    • Sapra, A.K., Khandelia, P. & Vijayraghavan, U. The splicing factor Prp17 interacts with the U2, U5 and U6 snRNPs and associates with the spliceosome pre-and post-catalysis. Biochem. J. 416, 365-374 (2008).
    • (2008) Biochem. J. , vol.416 , pp. 365-374
    • Sapra, A.K.1    Khandelia, P.2    Vijayraghavan, U.3
  • 29
    • 0036118353 scopus 로고    scopus 로고
    • Proteomics analysis reveals stable multiprotein complexes in both fssion and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA splicing factors, and snRNAs
    • Ohi, M.D. et al. Proteomics analysis reveals stable multiprotein complexes in both fssion and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA splicing factors, and snRNAs. Mol. Cell. Biol. 22, 2011-2024 (2002).
    • (2002) Mol. Cell. Biol , vol.22 , pp. 2011-2024
    • Ohi, M.D.1
  • 30
    • 0035252931 scopus 로고    scopus 로고
    • Coiled coils: A highly versatile protein folding motif
    • Burkhard, P., Stetefeld, J. & Strelkov, S.V. Coiled coils: a highly versatile protein folding motif. Trends Cell Biol. 11, 82-88 (2001).
    • (2001) Trends Cell Biol , vol.11 , pp. 82-88
    • Burkhard, P.1    Stetefeld, J.2    Strelkov, S.V.3
  • 31
    • 2542451914 scopus 로고    scopus 로고
    • Preferred amino acids and thermostability
    • Farias, S.T. & Bonato, M.C. Preferred amino acids and thermostability. Genet. Mol. Res. 2, 383-393 (2003).
    • (2003) Genet. Mol. Res , vol.2 , pp. 383-393
    • Farias, S.T.1    Bonato, M.C.2
  • 33
    • 0142187117 scopus 로고    scopus 로고
    • Corrim-based alignment for improved speed in single-particle image processing
    • Sander, B., Golas, M.M. & Stark, H. Corrim-based alignment for improved speed in single-particle image processing. J. Struct. Biol. 143, 219-228 (2003).
    • (2003) J. Struct. Biol , vol.143 , pp. 219-228
    • Sander, B.1    Golas, M.M.2    Stark, H.3
  • 34
    • 0019728717 scopus 로고
    • Use of multivariate statistics in analysing the images of biological macromolecules
    • van Heel, M. & Frank, J. Use of multivariate statistics in analysing the images of biological macromolecules. Ultramicroscopy 6, 187-194 (1981).
    • (1981) Ultramicroscopy , vol.6 , pp. 187-194
    • Van Heel, M.1    Frank, J.2
  • 35
    • 70350532246 scopus 로고    scopus 로고
    • Cwc25 is a novel splicing factor required after Prp2 and Yju2 to facilitate the frst catalytic reaction
    • Chiu, Y.F. et al. Cwc25 is a novel splicing factor required after Prp2 and Yju2 to facilitate the frst catalytic reaction. Mol. Cell. Biol. 29, 5671-5678 (2009).
    • (2009) Mol. Cell. Biol , vol.29 , pp. 5671-5678
    • Chiu, Y.F.1
  • 36
    • 0031878108 scopus 로고    scopus 로고
    • A potential role for U2AF-SAP 155 interactions in recruiting U2 snRNP to the branch site
    • Gozani, O., Potashkin, J. & Reed, R. A potential role for U2AF-SAP 155 interactions in recruiting U2 snRNP to the branch site. Mol. Cell. Biol. 18, 4752-4760 (1998).
    • (1998) Mol. Cell. Biol , vol.18 , pp. 4752-4760
    • Gozani, O.1    Potashkin, J.2    Reed, R.3
  • 37
    • 34250314386 scopus 로고    scopus 로고
    • Trans-splicing to spliceosomal U2 snRNA suggests disruption of branch site-U2 pairing during pre-mRNA splicing
    • Smith, D.J., Query, C.C. & Konarska, M.M. trans-splicing to spliceosomal U2 snRNA suggests disruption of branch site-U2 pairing during pre-mRNA splicing. Mol. Cell 26, 883-890 (2007).
    • (2007) Mol. Cell , vol.26 , pp. 883-890
    • Smith, D.J.1    Query, C.C.2    Konarska, M.M.3
  • 38
    • 0025941556 scopus 로고
    • U4 small nuclear RNA dissociates from a yeast spliceosome and does not participate in the subsequent splicing reaction
    • Yean, S.L. & Lin, R.J. U4 small nuclear RNA dissociates from a yeast spliceosome and does not participate in the subsequent splicing reaction. Mol. Cell. Biol. 11, 5571-5577 (1991).
    • (1991) Mol. Cell. Biol , vol.11 , pp. 5571-5577
    • Yean, S.L.1    Lin, R.J.2
  • 39
    • 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). (Pubitemid 20023238)
    • (1989) Genes and Development , vol.3 , Issue.12 B , pp. 2137-2150
    • Fabrizio, P.1    McPheeters, D.S.2    Abelson, J.3
  • 40
    • 37749007365 scopus 로고    scopus 로고
    • GraFix: Sample preparation for single-particle electron cryomicroscopy
    • Kastner, B. et al. GraFix: sample preparation for single-particle electron cryomicroscopy. Nat. Methods 5, 53-55 (2008).
    • (2008) Nat. Methods , vol.5 , pp. 53-55
    • Kastner, B.1
  • 41
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O. & Mann, M. Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem. 68, 850-858 (1996).
    • (1996) Anal. Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 42
    • 18344364097 scopus 로고    scopus 로고
    • The Orbitrap: A new mass spectrometer
    • Hu, Q. et al. The Orbitrap: a new mass spectrometer. J. Mass Spectrom. 40, 430-443 (2005).
    • (2005) J. Mass Spectrom , vol.40 , pp. 430-443
    • Hu, Q.1
  • 43
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high-density shaking cultures
    • Studier, F.W. Protein production by auto-induction in high-density shaking cultures. Protein Expr. Purif. 41, 207-234 (2005).
    • (2005) Protein Expr. Purif , vol.41 , pp. 207-234
    • Studier, F.W.1


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