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Volumn 467, Issue 7318, 2010, Pages 935-939

Single-molecule analysis of Mss116-mediated group II intron folding

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; DEAD BOX PROTEIN; MAGNESIUM ION; PROTEIN MSS116; UNCLASSIFIED DRUG;

EID: 78049234242     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature09422     Document Type: Article
Times cited : (72)

References (35)
  • 1
    • 18244424151 scopus 로고    scopus 로고
    • Quick guide: DEAD-box proteins
    • Linder, P. Quick guide: DEAD-box proteins. Curr. Biol. 10, R887 (2000).
    • (2000) Curr. Biol. , vol.10
    • Linder, P.1
  • 2
    • 0035476705 scopus 로고    scopus 로고
    • Escherichia coli DbpA is an RNA helicase that requires hairpin 92 of 23S rRNA
    • Diges, C. M. & Uhlenbeck, O. C. Escherichia coli DbpA is an RNA helicase that requires hairpin 92 of 23S rRNA. EMBO J. 20, 5503-5512 (2001).
    • (2001) EMBO J. , vol.20 , pp. 5503-5512
    • Diges, C.M.1    Uhlenbeck, O.C.2
  • 3
    • 11844297811 scopus 로고    scopus 로고
    • The splicing of yeast mitochondrial group i and group II introns requires a DEAD-box protein with RNA chaperone function
    • Huang, H. R. et al. The splicing of yeast mitochondrial group I and group II introns requires a DEAD-box protein with RNA chaperone function. Proc. Natl Acad. Sci. USA 102, 163-168 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 163-168
    • Huang, H.R.1
  • 4
    • 33847652952 scopus 로고    scopus 로고
    • DEADprotein that activates intron self-splicing without unwinding RNA
    • Solem, A., Zingler, N. &Pyle, A. M. A.DEADprotein that activates intron self-splicing without unwinding RNA. Mol. Cell 24, 611-617 (2006).
    • (2006) Mol. Cell , vol.24 , pp. 611-617
    • Solem, A.1    Zingler, N.2    Pyle, A.M.A.3
  • 5
    • 33845738802 scopus 로고    scopus 로고
    • Involvement of DEAD-box proteins in group i and group II intron splicing. Biochemical characterization of Mss116p, ATP hydrolysis-dependent and -independent mechanisms, and general RNA chaperone activity
    • Halls, C. et al. Involvement of DEAD-box proteins in group I and group II intron splicing. Biochemical characterization of Mss116p, ATP hydrolysis-dependent and -independent mechanisms, and general RNA chaperone activity. J. Mol. Biol. 365, 835-855 (2007).
    • (2007) J. Mol. Biol. , vol.365 , pp. 835-855
    • Halls, C.1
  • 6
    • 34948833173 scopus 로고    scopus 로고
    • DoDEAD-box proteins promote groupII intronsplicing without unwinding RNA?
    • Del Campo, M. et al.DoDEAD-box proteins promote groupII intronsplicing without unwinding RNA? Mol. Cell 28, 159-166 (2007).
    • (2007) Mol Cell , vol.28 , pp. 159-166
    • Del Campo, M.1
  • 7
    • 0038049910 scopus 로고    scopus 로고
    • Group II introns: Structure and catalytic versatility of large natural ribozymes
    • Lehmann, K. & Schmidt, U. Group II introns: structure and catalytic versatility of large natural ribozymes. Crit. Rev. Biochem. Mol. Biol. 38, 249-303 (2003).
    • (2003) Crit. Rev. Biochem. Mol. Biol. , vol.38 , pp. 249-303
    • Lehmann, K.1    Schmidt, U.2
  • 9
    • 0034910710 scopus 로고    scopus 로고
    • Coevolution of group II intron RNA structures with their intron-encoded reverse transcriptases
    • Toor, N., Hausner, G. & Zimmerly, S. Coevolution of group II intron RNA structures with their intron-encoded reverse transcriptases. RNA 7, 1142-1152 (2001).
    • (2001) RNA , vol.7 , pp. 1142-1152
    • Toor, N.1    Hausner, G.2    Zimmerly, S.3
  • 10
    • 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
  • 11
    • 0032103821 scopus 로고    scopus 로고
    • The architectural organization and mechanistic function of group II intron structural elements
    • Qin, P. Z. & Pyle, A. M. The architectural organization and mechanistic function of group II intron structural elements. Curr. Opin. Struct. Biol. 8, 301-308 (1998).
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 301-308
    • Qin, P.Z.1    Pyle, A.M.2
  • 12
    • 27844569938 scopus 로고    scopus 로고
    • 3rd ed.(eds Gesteland, R. F., Cech, T. R. & Atkins, J. F.) Chap. 17 469-505 (Cold Spring Harbor Laboratory Press)
    • Pyle, A. M. & Lambowitz, A. M. in The RNA World 3rd ed., Vol. 43 (eds Gesteland, R. F., Cech, T. R. & Atkins, J. F.) Chap. 17 469-505 (Cold Spring Harbor Laboratory Press, 2006).
    • (2006) The RNA World , vol.43
    • Pyle, A.M.1    Lambowitz, A.M.2
  • 13
    • 0026695012 scopus 로고
    • Group II introns deleted for multiple substructures retain self-splicing activity
    • Koch, J. L., Boulanger, S. C., Dib-Hajj, S. D., Hebbar, S. K. & Perlman, P. S. Group II introns deleted for multiple substructures retain self-splicing activity. Mol. Cell. Biol. 12, 1950-1958 (1992).
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 1950-1958
    • Koch, J.L.1    Boulanger, S.C.2    Dib-Hajj, S.D.3    Hebbar, S.K.4    Perlman, P.S.5
  • 14
    • 0028904152 scopus 로고
    • Conversion of a group II intron into a new multipleturnover ribozyme that selectively cleaves oligonucleotides: Elucidation of reaction mechanism and structure/function relationships
    • Michels, W. J. Jr & Pyle, A. M. Conversion of a group II intron into a new multiplet urnover ribozyme that selectively cleaves oligonucleotides: elucidation of reaction mechanism and structure/function relationships. Biochemistry 34, 2965-2977 (1995).
    • (1995) Biochemistry , vol.34 , pp. 2965-2977
    • Michels Jr., W.J.1    Pyle, A.M.2
  • 15
    • 0030936233 scopus 로고    scopus 로고
    • Stopped-flow fluorescence spectroscopy of a group II intron ribozyme reveals that domain 1 is an independent folding unit with a requirement for specificMg21ionsinthe tertiary structure
    • Qin, P. Z. & Pyle, A.M. Stopped-flow fluorescence spectroscopy of a group II intron ribozyme reveals that domain 1 is an independent folding unit with a requirement for specificMg21ionsinthe tertiary structure. Biochemistry 36,4718-4730(1997).
    • (1997) Biochemistry , vol.36 , pp. 4718-4730
    • Qin, P.Z.1    Pyle, A.M.2
  • 16
    • 29244449617 scopus 로고    scopus 로고
    • An obligate intermediate along the slow folding pathway of a group II intron ribozyme
    • Su, L. J., Waldsich, C. & Pyle, A. M. An obligate intermediate along the slow folding pathway of a group II intron ribozyme. Nucleic Acids Res. 33, 6674-6687 (2005).
    • (2005) Nucleic Acids Res. , vol.33 , pp. 6674-6687
    • Su, L.J.1    Waldsich, C.2    Pyle, A.M.3
  • 18
    • 71949084158 scopus 로고    scopus 로고
    • Ca21 induces the formation of two distinct subpopulations of group II intronmolecules
    • Steiner, M., Rueda, D. & Sigel, R. K. O. Ca21 induces the formation of two distinct subpopulations of group II intronmolecules. Angew. Chem. Int. Ed. 48, 9739-9742 (2009).
    • (2009) Angew. Chem. Int. Ed. , vol.48 , pp. 9739-9742
    • Steiner, M.1    Rueda, D.2    Sigel, R.K.O.3
  • 19
    • 0242381359 scopus 로고    scopus 로고
    • Effects of maturase binding and Mg21 concentration on group II intron RNA folding investigated by UV cross-linking
    • Noah, J. W. & Lambowitz, A. M. Effects of maturase binding and Mg21 concentration on group II intron RNA folding investigated by UV cross-linking. Biochemistry 42, 12466-12480 (2003).
    • (2003) Biochemistry , vol.42 , pp. 12466-12480
    • Noah, J.W.1    Lambowitz, A.M.2
  • 20
    • 0029384106 scopus 로고
    • Escherichia coli protein StpA stimulates self-splicing by promoting RNA assembly in vitro
    • Zhang, A., Derbyshire, V., Salvo, J. L. & Belfort, M. Escherichia coli protein StpA stimulates self-splicing by promoting RNA assembly in vitro. RNA 1, 783-793 (1995).
    • (1995) RNA , vol.1 , pp. 783-793
    • Zhang, A.1    Derbyshire, V.2    Salvo, J.L.3    Belfort, M.4
  • 21
    • 0033169013 scopus 로고    scopus 로고
    • Assaying RNA chaperone activity in vivo using a novel RNA folding trap
    • Clodi, E., Semrad, K. & Schroeder, R. Assaying RNA chaperone activity in vivo using a novel RNA folding trap. EMBO J. 18, 3776-3782 (1999).
    • (1999) EMBO J. , vol.18 , pp. 3776-3782
    • Clodi, E.1    Semrad, K.2    Schroeder, R.3
  • 22
    • 77649337588 scopus 로고    scopus 로고
    • Protein-facilitated folding of group II intron ribozymes
    • Fedorova, O., Solem, A. & Pyle, A. M. Protein-facilitated folding of group II intron ribozymes. J. Mol. Biol. 397, 799-813 (2010).
    • (2010) J. Mol. Biol. , vol.397 , pp. 799-813
    • Fedorova, O.1    Solem, A.2    Pyle, A.M.3
  • 23
    • 33846096930 scopus 로고    scopus 로고
    • A folding control element for tertiary collapse of a group II intron ribozyme
    • Waldsich, C. &Pyle, A. M. A folding control element for tertiary collapse of a group II intron ribozyme. Nature Struct. Mol. Biol. 14, 37-44 (2007).
    • (2007) Nature Struct. Mol. Biol. , vol.14 , pp. 37-44
    • Waldsich, C.1    Pyle, A.M.2
  • 24
    • 33846637337 scopus 로고    scopus 로고
    • Group II intron folding under nearphysiological conditions: Collapsing to the near-native state
    • Fedorova, O., Waldsich, C. & Pyle, A. M. Group II intron folding under nearphysiological conditions: collapsing to the near-native state. J. Mol. Biol. 366, 1099-1114 (2007).
    • (2007) J. Mol. Biol. , vol.366 , pp. 1099-1114
    • Fedorova, O.1    Waldsich, C.2    Pyle, A.M.3
  • 25
    • 23144448275 scopus 로고    scopus 로고
    • Nucleic Acid Chaperone Activity of HIV-1 Nucleocapsid Protein: Critical Role in Reverse Transcription and Molecular Mechanism
    • DOI 10.1016/S0079-6603(05)80006-6, PII S0079660305800066
    • Levin, J. G., Guo, J., Rouzina, I. & Musier-Forsyth, K. Nucleic acid chaperone activity of HIV-1 nucleocapsid protein: critical role in reverse transcription and molecular mechanism. Prog. Nucleic Acid Res. Mol. Biol. 80, 217-286 (2005). (Pubitemid 43574891)
    • (2005) Progress in Nucleic Acid Research and Molecular Biology , vol.80 , pp. 217-286
    • Levin, J.G.1    Guo, J.2    Rouzina, I.3    Musier-Forsyth, K.4
  • 26
    • 77749270589 scopus 로고    scopus 로고
    • RNA looping by PTB: Evidence using FRET and NMR spectroscopy and for a role in splicing repression
    • Lamichhane, R. et al. RNA looping by PTB: evidence using FRET and NMR spectroscopy and for a role in splicing repression. Proc. Natl Acad. Sci. USA 107, 4105-4110 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 4105-4110
    • Lamichhane, R.1
  • 27
    • 70350699443 scopus 로고    scopus 로고
    • Effect of salt and RNA structure on annealing and strand displacement by Hfq
    • Hopkins, J. F., Panja, S., McNeil, S. A. & Woodson, S. A. Effect of salt and RNA structure on annealing and strand displacement by Hfq. Nucleic Acids Res. 37, 6205-6213 (2009).
    • (2009) Nucleic Acids Res. , vol.37 , pp. 6205-6213
    • Hopkins, J.F.1    Panja, S.2    McNeil, S.A.3    Woodson, S.A.4
  • 28
    • 33746747438 scopus 로고    scopus 로고
    • Analysis of single-molecule FRET trajectories using hidden Markov modeling
    • McKinney, S. A., Joo, C. & Ha, T. Analysis of single-molecule FRET trajectories using hidden Markov modeling. Biophys. J. 91, 1941-1951 (2006).
    • (2006) Biophys. J. , vol.91 , pp. 1941-1951
    • McKinney, S.A.1    Joo, C.2    Ha, T.3
  • 29
    • 77951625452 scopus 로고    scopus 로고
    • Structure-guided mutational analysis of a yeast DEAD-box protein involved in mitochondrial RNA splicing
    • Bifano, A. L., Turk, E. M. & Caprara, M. G. Structure-guided mutational analysis of a yeast DEAD-box protein involved in mitochondrial RNA splicing. J. Mol. Biol. 398, 429-443 (2010).
    • (2010) J. Mol. Biol. , vol.398 , pp. 429-443
    • Bifano, A.L.1    Turk, E.M.2    Caprara, M.G.3
  • 30
    • 58149481225 scopus 로고    scopus 로고
    • ATP hydrolysis is required for DEAD-box protein recycling but not for duplex unwinding
    • Liu, F., Putnam, A. &Jankowsky, E. ATP hydrolysis is required for DEAD-box protein recycling but not for duplex unwinding. Proc. Natl Acad. Sci. USA 105, 20209-20214 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 20209-20214
    • Liu, F.1    Putnam, A.2    Jankowsky, E.3
  • 31
    • 78049293801 scopus 로고    scopus 로고
    • Dual roles for the Mss116 cofactor during splicing of the ai5c group II intron
    • (in the press)
    • Zingler, N., Solem, A. & Pyle, A. M. Dual roles for the Mss116 cofactor during splicing of the ai5c group II intron. Nucleic Acids Res. (in the press) (2010).
    • (2010) Nucleic Acids Res.
    • Zingler, N.1    Solem, A.2    Pyle, A.M.3
  • 32
    • 70349281455 scopus 로고    scopus 로고
    • RNA folding dynamics by single-molecule fluorescence resonance energy transfer
    • Zhao, R. & Rueda, D. RNA folding dynamics by single-molecule fluorescence resonance energy transfer. Methods 49, 112-117 (2009).
    • (2009) Methods , vol.49 , pp. 112-117
    • Zhao, R.1    Rueda, D.2
  • 33
    • 0037057630 scopus 로고    scopus 로고
    • Initiation and re-initiation ofDNAunwinding by the Escherichia coli Rep helicase
    • Ha, T. et al. Initiation and re-initiation ofDNAunwinding by the Escherichia coli Rep helicase. Nature 419, 638-641 (2002).
    • (2002) Nature , vol.419 , pp. 638-641
    • Ha, T.1
  • 34
    • 75849150495 scopus 로고    scopus 로고
    • Single molecule measurements of synthesis by DNA polymerase with base-pair resolution
    • Christian, T. D., Romano, L. J. & Rueda, D. Single molecule measurements of synthesis by DNA polymerase with base-pair resolution. Proc. Natl Acad. Sci. USA 106, 21109-21114 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 21109-21114
    • Christian, T.D.1    Romano, L.J.2    Rueda, D.3
  • 35
    • 0019307789 scopus 로고
    • The role of ATP in in vitro vaccinia virus RNA synthesis effects of AMP-PNP and ATPcS
    • Shuman, S., Spencer, E., Furneaux, H. & Hurwitz, J. The role of ATP in in vitro vaccinia virus RNA synthesis effects of AMP-PNP and ATPcS. J. Biol. Chem. 255, 5396-5403 (1980).
    • (1980) J. Biol. Chem. , vol.255 , pp. 5396-5403
    • Shuman, S.1    Spencer, E.2    Furneaux, H.3    Hurwitz, J.4


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