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Volumn 103, Issue 12, 2012, Pages 2541-2548

Single-molecule observation of the induction of k-turn RNA structure on binding L7Ae protein

Author keywords

[No Author keywords available]

Indexed keywords

ARCHAEAL PROTEIN; ARCHAEAL RNA; IMMOBILIZED PROTEIN;

EID: 84871324763     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2012.11.006     Document Type: Article
Times cited : (25)

References (39)
  • 1
    • 0035423087 scopus 로고    scopus 로고
    • The kink-turn: A new RNA secondary structure motif
    • DOI 10.1093/emboj/20.15.4214
    • D.J. Klein, and T.M. Schmeing T.A. Steitz The kink-turn: a new RNA secondary structure motif EMBO J. 20 2001 4214 4221 (Pubitemid 32751837)
    • (2001) EMBO Journal , vol.20 , Issue.15 , pp. 4214-4221
    • Klein, D.J.1    Schmeing, T.M.2    Moore, P.B.3    Steitz, T.A.4
  • 2
    • 33846441637 scopus 로고    scopus 로고
    • The role of specific 2′-hydroxyl groups in the stabilization of the folded conformation of kink-turn RNA
    • DOI 10.1261/rna.285707
    • J. Liu, and D.M.J. Lilley The role of specific 2′-hydroxyl groups in the stabilization of the folded conformation of kink-turn RNA RNA 13 2007 200 210 (Pubitemid 46147896)
    • (2007) RNA , vol.13 , Issue.2 , pp. 200-210
    • Liu, J.1    Lilley, D.M.J.2
  • 3
    • 47049124440 scopus 로고    scopus 로고
    • The importance of GṡA hydrogen bonding in the metal ion- and protein-induced folding of a kink turn RNA
    • B. Turner, and D.M. Lilley The importance of GṡA hydrogen bonding in the metal ion- and protein-induced folding of a kink turn RNA J. Mol. Biol. 381 2008 431 442
    • (2008) J. Mol. Biol. , vol.381 , pp. 431-442
    • Turner, B.1    Lilley, D.M.2
  • 4
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
    • DOI 10.1126/science.289.5481.905
    • N. Ban, and P. Nissen T.A. Steitz The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution Science 289 2000 905 920 (Pubitemid 30659939)
    • (2000) Science , vol.289 , Issue.5481 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 6
    • 0028225137 scopus 로고
    • A novel RNA-binding motif in omnipotent suppressors of translation termination, ribosomal proteins and a ribosome modification enzyme?
    • E.V. Koonin, P. Bork, and C. Sander A novel RNA-binding motif in omnipotent suppressors of translation termination, ribosomal proteins and a ribosome modification enzyme? Nucleic Acids Res. 22 1994 2166 2167 (Pubitemid 24192921)
    • (1994) Nucleic Acids Research , vol.22 , Issue.11 , pp. 2166-2167
    • Koonin, E.V.1    Bork, P.2    Sander, C.3
  • 7
    • 0033229873 scopus 로고    scopus 로고
    • Functional interaction of a novel 15.5kD [U4/U6·U5] tri-snRNP protein with the 5' stem-loop of U4 snRNA
    • DOI 10.1093/emboj/18.21.6119
    • S. Nottrott, and K. Hartmuth R. Lührmann Functional interaction of a novel 15.5kD [U4/U6.U5] tri-snRNP protein with the 5′ stem-loop of U4 snRNA EMBO J. 18 1999 6119 6133 (Pubitemid 29515687)
    • (1999) EMBO Journal , vol.18 , Issue.21 , pp. 6119-6133
    • Nottrott, S.1    Hartmuth, K.2    Fabrizio, P.3    Urlaub, H.4    Vidovic, I.5    Ficner, R.6    Luhrmann, R.7
  • 8
    • 84863338217 scopus 로고    scopus 로고
    • YbxF and YlxQ are bacterial homologs of L7Ae and bind K-turns but not K-loops
    • N.J. Baird, and J. Zhang A.R. Ferré-D'Amaré YbxF and YlxQ are bacterial homologs of L7Ae and bind K-turns but not K-loops RNA 18 2012 759 770
    • (2012) RNA , vol.18 , pp. 759-770
    • Baird, N.J.1    Zhang, J.2    Ferré-D'Amaré, A.R.3
  • 9
    • 0030604698 scopus 로고    scopus 로고
    • Site-specific ribose methylation of preribosomal RNA: A novel function for small nucleolar RNAs
    • DOI 10.1016/S0092-8674(00)81308-2
    • Z. Kiss-László, and Y. Henry T. Kiss Site-specific ribose methylation of preribosomal RNA: a novel function for small nucleolar RNAs Cell 85 1996 1077 1088 (Pubitemid 26231174)
    • (1996) Cell , vol.85 , Issue.7 , pp. 1077-1088
    • Kiss-Laszlo, Z.1    Henry, Y.2    Bachellerie, J.-P.3    Caizergues-Ferrer, M.4    Kiss, T.5
  • 10
    • 0030711050 scopus 로고    scopus 로고
    • Site-specific pseudouridine formation in preribosomal RNA is guided by small nucleolar RNAs
    • P. Ganot, M.L. Bortolin, and T. Kiss Site-specific pseudouridine formation in preribosomal RNA is guided by small nucleolar RNAs Cell 89 1997 799 809 (Pubitemid 27516183)
    • (1997) Cell , vol.89 , Issue.5 , pp. 799-809
    • Ganot, P.1    Bortolin, M.-L.2    Kiss, T.3
  • 11
    • 2342475659 scopus 로고    scopus 로고
    • Molecular basis of box C/D RNA-protein interactions: Cocrystal structure of archaeal L7Ae and a box C/D RNA
    • DOI 10.1016/j.str.2004.02.033, PII S0969212604001169
    • T. Moore, and Y. Zhang H. Li Molecular basis of box C/D RNA-protein interactions; cocrystal structure of archaeal L7Ae and a box C/D RNA Structure 12 2004 807 818 (Pubitemid 38595769)
    • (2004) Structure , vol.12 , Issue.5 , pp. 807-818
    • Moore, T.1    Zhang, Y.2    Fenley, M.O.3    Li, H.4
  • 12
    • 22244460838 scopus 로고    scopus 로고
    • The crystal structure of the Methanocaldococcus jannaschii multifunctional L7Ae RNA-binding protein reveals an induced-fit interaction with the box C/D RNAs
    • DOI 10.1021/bi050568q
    • J. Suryadi, and E.J. Tran B.A. Brown 2nd The crystal structure of the Methanocaldococcus jannaschii multifunctional L7Ae RNA-binding protein reveals an induced-fit interaction with the box C/D RNAs Biochemistry 44 2005 9657 9672 (Pubitemid 40994360)
    • (2005) Biochemistry , vol.44 , Issue.28 , pp. 9657-9672
    • Suryadi, J.1    Tran, E.J.2    Maxwell, E.S.3    Brown II, B.A.4
  • 13
    • 2342638215 scopus 로고    scopus 로고
    • Structure of protein L7Ae bound to a K-turn derived from an archaeal box H/ACA sRNA at 1.8 Å resolution
    • DOI 10.1016/j.str.2004.03.015, PII S0969212604000966
    • T. Hamma, and A.R. Ferré-D'Amaré Structure of protein L7Ae bound to a K-turn derived from an archaeal box H/ACA sRNA at 1.8 Å resolution Structure 12 2004 893 903 (Pubitemid 38595777)
    • (2004) Structure , vol.12 , Issue.5 , pp. 893-903
    • Hamma, T.1    Ferre-D'Amare, A.R.2
  • 14
    • 0034509631 scopus 로고    scopus 로고
    • Crystal structure of the spliceosomal 15.5kD protein bound to a U4 snRNA fragment
    • DOI 10.1016/S1097-2765(00)00131-3
    • I. Vidovic, and S. Nottrott R. Ficner Crystal structure of the spliceosomal 15.5kD protein bound to a U4 snRNA fragment Mol. Cell 6 2000 1331 1342 (Pubitemid 32045926)
    • (2000) Molecular Cell , vol.6 , Issue.6 , pp. 1331-1342
    • Vidovic, I.1    Nottrott, S.2    Hartmuth, K.3    Luhrmann, R.4    Ficner, R.5
  • 15
    • 0141940267 scopus 로고    scopus 로고
    • Biochemical characterization of the kink-turn RNA motif
    • DOI 10.1093/nar/gkg760
    • S. Matsumura, Y. Ikawa, and T. Inoue Biochemical characterization of the kink-turn RNA motif Nucleic Acids Res. 31 2003 5544 5551 (Pubitemid 37441924)
    • (2003) Nucleic Acids Research , vol.31 , Issue.19 , pp. 5544-5551
    • Matsumura, S.1    Ikawa, Y.2    Inoue, T.3
  • 16
    • 1642458421 scopus 로고    scopus 로고
    • The kink-turn motif in RNA is dimorphic, and metal ion-dependent
    • DOI 10.1261/rna.5176604
    • T.A. Goody, and S.E. Melcher D.M. Lilley The kink-turn motif in RNA is dimorphic, and metal ion-dependent RNA 10 2004 254 264 (Pubitemid 38129830)
    • (2004) RNA , vol.10 , Issue.2 , pp. 254-264
    • Goody, T.A.1    Melcher, S.E.2    Norman, D.G.3    Lilley, D.M.J.4
  • 17
    • 80052447978 scopus 로고    scopus 로고
    • RNA tertiary interactions in a riboswitch stabilize the structure of a kink turn
    • K.T. Schroeder, P. Daldrop, and D.M.J. Lilley RNA tertiary interactions in a riboswitch stabilize the structure of a kink turn Structure 19 2011 1233 1240
    • (2011) Structure , vol.19 , pp. 1233-1240
    • Schroeder, K.T.1    Daldrop, P.2    Lilley, D.M.J.3
  • 18
    • 22244483207 scopus 로고    scopus 로고
    • Induced fit of RNA on binding the L7Ae protein to the kink-turn motif
    • DOI 10.1261/rna.2680605
    • B. Turner, and S.E. Melcher D.M. Lilley Induced fit of RNA on binding the L7Ae protein to the kink-turn motif RNA 11 2005 1192 1200 (Pubitemid 41132391)
    • (2005) RNA , vol.11 , Issue.8 , pp. 1192-1200
    • Turner, B.1    Melcher, S.E.2    Wilson, T.J.3    Norman, D.G.4    Lilley, D.M.J.5
  • 20
    • 0001858251 scopus 로고
    • Application of a theory of enzyme specificity to protein synthesis
    • D.E. Koshland Application of a theory of enzyme specificity to protein synthesis Proc. Natl. Acad. Sci. USA 44 1958 98 104
    • (1958) Proc. Natl. Acad. Sci. USA , vol.44 , pp. 98-104
    • Koshland, D.E.1
  • 22
    • 0037114646 scopus 로고    scopus 로고
    • Molecular dynamics simulation studies of induced fit and conformational capture in U1A-RNA binding: Do molecular substates code for specificity?
    • DOI 10.1002/bip.10251
    • F. Pitici, D.L. Beveridge, and A.M. Baranger Molecular dynamics simulation studies of induced fit and conformational capture in U1A-RNA binding: do molecular substates code for specificity? Biopolymers 65 2002 424 435 (Pubitemid 35423738)
    • (2002) Biopolymers , vol.65 , Issue.6 , pp. 424-435
    • Pitici, F.1    Beveridge, D.L.2    Baranger, A.M.3
  • 23
    • 49649084492 scopus 로고    scopus 로고
    • Dynamic energy landscape view of coupled binding and protein conformational change: Induced-fit versus population-shift mechanisms
    • K. Okazaki, and S. Takada Dynamic energy landscape view of coupled binding and protein conformational change: induced-fit versus population-shift mechanisms Proc. Natl. Acad. Sci. USA 105 2008 11182 11187
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 11182-11187
    • Okazaki, K.1    Takada, S.2
  • 24
    • 65249090946 scopus 로고    scopus 로고
    • Selected-fit versus induced-fit protein binding: Kinetic differences and mutational analysis
    • T.R. Weikl, and C. von Deuster Selected-fit versus induced-fit protein binding: kinetic differences and mutational analysis Proteins 75 2009 104 110
    • (2009) Proteins , vol.75 , pp. 104-110
    • Weikl, T.R.1    Von Deuster, C.2
  • 25
    • 69549120472 scopus 로고    scopus 로고
    • Conformational selection or induced fit: A flux description of reaction mechanism
    • G.G. Hammes, Y.C. Chang, and T.G. Oas Conformational selection or induced fit: a flux description of reaction mechanism Proc. Natl. Acad. Sci. USA 106 2009 13737 13741
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 13737-13741
    • Hammes, G.G.1    Chang, Y.C.2    Oas, T.G.3
  • 26
    • 77957231785 scopus 로고    scopus 로고
    • Induced fit, conformational selection and independent dynamic segments: An extended view of binding events
    • P. Csermely, R. Palotai, and R. Nussinov Induced fit, conformational selection and independent dynamic segments: an extended view of binding events Trends Biochem. Sci. 35 2010 539 546
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 539-546
    • Csermely, P.1    Palotai, R.2    Nussinov, R.3
  • 27
    • 77949587817 scopus 로고    scopus 로고
    • From induced fit to conformational selection: A continuum of binding mechanism controlled by the timescale of conformational transitions
    • H.X. Zhou From induced fit to conformational selection: a continuum of binding mechanism controlled by the timescale of conformational transitions Biophys. J. 98 2010 L15 L17
    • (2010) Biophys. J. , vol.98
    • Zhou, H.X.1
  • 28
    • 33645077057 scopus 로고    scopus 로고
    • Molecular dynamics simulation studies of a protein-RNA complex with a selectively modified binding interface
    • Y. Zhao, and B.L. Kormos A.M. Baranger Molecular dynamics simulation studies of a protein-RNA complex with a selectively modified binding interface Biopolymers 81 2006 256 269
    • (2006) Biopolymers , vol.81 , pp. 256-269
    • Zhao, Y.1    Kormos, B.L.2    Baranger, A.M.3
  • 29
    • 77951170511 scopus 로고    scopus 로고
    • Induced fit or conformational selection for RNA/U1A folding
    • F. Qin, and Y. Chen H.F. Chen Induced fit or conformational selection for RNA/U1A folding RNA 16 2010 1053 1061
    • (2010) RNA , vol.16 , pp. 1053-1061
    • Qin, F.1    Chen, Y.2    Chen, H.F.3
  • 30
    • 74249115345 scopus 로고    scopus 로고
    • Topology links RNA secondary structure with global conformation, dynamics, and adaptation
    • M.H. Bailor, X. Sun, and H.M. Al-Hashimi Topology links RNA secondary structure with global conformation, dynamics, and adaptation Science 327 2010 202 206
    • (2010) Science , vol.327 , pp. 202-206
    • Bailor, M.H.1    Sun, X.2    Al-Hashimi, H.M.3
  • 31
    • 79958136745 scopus 로고    scopus 로고
    • A role for both conformational selection and induced fit in ligand binding by the LAO protein
    • D.A. Silva, and G.R. Bowman X. Huang A role for both conformational selection and induced fit in ligand binding by the LAO protein PLOS Comput. Biol. 7 2011 e1002054
    • (2011) PLOS Comput. Biol. , vol.7 , pp. 1002054
    • Silva, D.A.1    Bowman, G.R.2    Huang, X.3
  • 32
    • 33846898497 scopus 로고    scopus 로고
    • Interplay of 'induced fit' and preorganization in the ligand induced folding of the aptamer domain of the guanine binding riboswitch
    • DOI 10.1093/nar/gkl1094
    • J. Noeske, and J. Buck J. Wöhnert Interplay of 'induced fit' and preorganization in the ligand induced folding of the aptamer domain of the guanine binding riboswitch Nucleic Acids Res. 35 2007 572 583 (Pubitemid 46232073)
    • (2007) Nucleic Acids Research , vol.35 , Issue.2 , pp. 572-583
    • Noeske, J.1    Buck, J.2    Furtig, B.3    Nasiri, H.R.4    Schwalbe, H.5    Wohnert, J.6
  • 34
    • 35548976322 scopus 로고    scopus 로고
    • Open-to-closed transition in apo maltose-binding protein observed by paramagnetic NMR
    • DOI 10.1038/nature06232, PII NATURE06232
    • C. Tang, C.D. Schwieters, and G.M. Clore Open-to-closed transition in apo maltose-binding protein observed by paramagnetic NMR Nature 449 2007 1078 1082 (Pubitemid 350014601)
    • (2007) Nature , vol.449 , Issue.7165 , pp. 1078-1082
    • Tang, C.1    Schwieters, C.D.2    Clore, G.M.3
  • 35
    • 73349117207 scopus 로고    scopus 로고
    • Conformational selection and induced fit mechanism underlie specificity in noncovalent interactions with ubiquitin
    • T. Wlodarski, and B. Zagrovic Conformational selection and induced fit mechanism underlie specificity in noncovalent interactions with ubiquitin Proc. Natl. Acad. Sci. USA 106 2009 19346 19351
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 19346-19351
    • Wlodarski, T.1    Zagrovic, B.2
  • 36
    • 76549109225 scopus 로고    scopus 로고
    • Millisecond timescale fluctuations in dihydrofolate reductase are exquisitely sensitive to the bound ligands
    • D.D. Boehr, and D. McElheny P.E. Wright Millisecond timescale fluctuations in dihydrofolate reductase are exquisitely sensitive to the bound ligands Proc. Natl. Acad. Sci. USA 107 2010 1373 1378
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 1373-1378
    • Boehr, D.D.1    McElheny, D.2    Wright, P.E.3
  • 37
    • 49149135789 scopus 로고
    • Deoxynucleoside phosphoramidites - A new class of key intermediates for deoxypolynucleotide synthesis
    • S.L. Beaucage, and M.H. Caruthers Deoxynucleoside phosphoramidites - a new class of key intermediates for deoxypolynucleotide synthesis Tetrahedron Lett. 22 1981 1859 1862
    • (1981) Tetrahedron Lett. , vol.22 , pp. 1859-1862
    • Beaucage, S.L.1    Caruthers, M.H.2
  • 38
    • 0035916297 scopus 로고    scopus 로고
    • Importance of specific nucleotides in the folding of the natural form of the hairpin ribozyme
    • DOI 10.1021/bi002644p
    • T.J. Wilson, and Z.-Y. Zhao D.M. Lilley Importance of specific nucleotides in the folding of the natural form of the hairpin ribozyme Biochemistry 40 2001 2291 2302 (Pubitemid 32165701)
    • (2001) Biochemistry , vol.40 , Issue.7 , pp. 2291-2302
    • Wilson, T.J.1    Zhao, Z.-Y.2    Maxwell, K.3    Kontogiannis, L.4    Lilley, D.M.J.5
  • 39
    • 0034807927 scopus 로고    scopus 로고
    • Single-molecule fluorescence resonance energy transfer
    • DOI 10.1006/meth.2001.1217
    • T. Ha Single-molecule fluorescence resonance energy transfer Methods 25 2001 78 86 (Pubitemid 32905290)
    • (2001) Methods , vol.25 , Issue.1 , pp. 78-86
    • Ha, T.1


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