메뉴 건너뛰기




Volumn 5, Issue 7, 1999, Pages 947-958

Influence of specific mutations on the thermal stability of the td group I intron in vitro and on its splicing efficiency in vivo: A comparative study

Author keywords

Cooperative folding; Group I intron; Secondary structure; Tertiary structure; UV melting

Indexed keywords

BACTERIAL RNA;

EID: 0032991584     PISSN: 13558382     EISSN: None     Source Type: Journal    
DOI: 10.1017/S1355838299990477     Document Type: Article
Times cited : (25)

References (50)
  • 1
    • 0016030365 scopus 로고
    • Trimethoprim action and its analogy with thymine starvation
    • Amyes SGB, Smith JT. 1974. Trimethoprim action and its analogy with thymine starvation. Antimicrob Agents Chemother 5:169-178.
    • (1974) Antimicrob Agents Chemother , vol.5 , pp. 169-178
    • Amyes, S.G.B.1    Smith, J.T.2
  • 2
    • 0027434244 scopus 로고
    • Thermal unfolding of a group I ribozyme: The low-temperature transition is primarily disruption of tertiary structure
    • Banerjee AR, Jaeger JA, Turner, DH. 1993. Thermal unfolding of a group I ribozyme: The low-temperature transition is primarily disruption of tertiary structure. Biochemistry 32:153-163.
    • (1993) Biochemistry , vol.32 , pp. 153-163
    • Banerjee, A.R.1    Jaeger, J.A.2    Turner, D.H.3
  • 3
    • 0026649231 scopus 로고
    • Directed evolution of an RNA enzyme
    • Beaudry AA, Joyce GF. 1992. Directed evolution of an RNA enzyme. Science 257:635-641.
    • (1992) Science , vol.257 , pp. 635-641
    • Beaudry, A.A.1    Joyce, G.F.2
  • 4
    • 0023512003 scopus 로고
    • Genetic delineation of functional components of the group I intron in the phage T4 td gene
    • Belfort M, Chandry PS, Pedersen-Lane J. 1987. Genetic delineation of functional components of the group I intron in the phage T4 td gene. Cold Spring Harbor Symp Quant Biol 52:181-192.
    • (1987) Cold Spring Harbor Symp Quant Biol , vol.52 , pp. 181-192
    • Belfort, M.1    Chandry, P.S.2    Pedersen-Lane, J.3
  • 5
    • 0025286439 scopus 로고
    • Genetic and molecular analysis of RNA splicing in Escherichia coli
    • Belfort M, Ehrenmann K, Chandry PS. 1990. Genetic and molecular analysis of RNA splicing in Escherichia coli Methods Enzymol 181:521-539.
    • (1990) Methods Enzymol , vol.181 , pp. 521-539
    • Belfort, M.1    Ehrenmann, K.2    Chandry, P.S.3
  • 6
    • 0020527037 scopus 로고
    • Purification and properties of T4 phage thymidylate synthase produced by the cloned gene in an amplification vector
    • Belfort M, Moelleken A, Maley GF, Maley F. 1983. Purification and properties of T4 phage thymidylate synthase produced by the cloned gene in an amplification vector. J Biol Chem 258:2045-2051.
    • (1983) J Biol Chem , vol.258 , pp. 2045-2051
    • Belfort, M.1    Moelleken, A.2    Maley, G.F.3    Maley, F.4
  • 8
    • 0033564415 scopus 로고    scopus 로고
    • Analysis of the cooperative unfolding of the td intron of bacteriophage T4
    • In press
    • Brion P, Michel F, Schroeder R, Westhof E. 1999. Analysis of the cooperative unfolding of the td intron of bacteriophage T4. Nucleic Acids Res 27. In press.
    • (1999) Nucleic Acids Res , vol.27
    • Brion, P.1    Michel, F.2    Schroeder, R.3    Westhof, E.4
  • 10
    • 0030582766 scopus 로고    scopus 로고
    • A tyrosyl-tRNA synthetase recognizes a conserved tRNA-like structural motif in the group I intron catalytic core
    • Caprara MG, Lehnert V, Lambowitz AM, Westhof E. 1996. A tyrosyl-tRNA synthetase recognizes a conserved tRNA-like structural motif in the group I intron catalytic core. Cell 87:1135-1145.
    • (1996) Cell , vol.87 , pp. 1135-1145
    • Caprara, M.G.1    Lehnert, V.2    Lambowitz, A.M.3    Westhof, E.4
  • 12
    • 0024214064 scopus 로고
    • Conserved sequences and structures of group I introns: Building an active site for RNA catalysis - A review
    • Cech TR. 1988. Conserved sequences and structures of group I introns: Building an active site for RNA catalysis - a review. Gene 73:259-271.
    • (1988) Gene , vol.73 , pp. 259-271
    • Cech, T.R.1
  • 13
    • 0025367254 scopus 로고
    • Self-splicing of group I introns
    • Cech TR. 1990. Self-splicing of group I introns. Annu Rev Biochem 59:543-568.
    • (1990) Annu Rev Biochem , vol.59 , pp. 543-568
    • Cech, T.R.1
  • 14
    • 0028441183 scopus 로고
    • Representation of the secondary and tertiary structure of group I introns
    • Cech TR, Damberger SH, Gutell R. 1994. Representation of the secondary and tertiary structure of group I introns. Nat Struct Biol 1:273-280.
    • (1994) Nat Struct Biol , vol.1 , pp. 273-280
    • Cech, T.R.1    Damberger, S.H.2    Gutell, R.3
  • 15
    • 0023441491 scopus 로고
    • Activation of a cryptic 5′ splice site in the upstream exon of the phage T4 td transcript: Exon context, missplicing and mRNA deletion in a fidelity mutant
    • Chandry PS, Belfort M. 1987. Activation of a cryptic 5′ splice site in the upstream exon of the phage T4 td transcript: Exon context, missplicing and mRNA deletion in a fidelity mutant. Genes & Dev 1:1028-1037.
    • (1987) Genes & Dev , vol.1 , pp. 1028-1037
    • Chandry, P.S.1    Belfort, M.2
  • 16
    • 0022512235 scopus 로고
    • Characterization of the intron in the phage T4 thymidylate synthase gene and evidence for its self-excision from the primary transcript
    • Chu F, Maley GF, West DK, Belfort M, Maley F. 1986. Characterization of the intron in the phage T4 thymidylate synthase gene and evidence for its self-excision from the primary transcript. Cell 45:157-166.
    • (1986) Cell , vol.45 , pp. 157-166
    • Chu, F.1    Maley, G.F.2    West, D.K.3    Belfort, M.4    Maley, F.5
  • 17
    • 0028276865 scopus 로고
    • Escherichia coli proteins, including ribosomal protein S12, facilitate in vitro splicing of phage T4 introns by acting as RNA chaperones
    • Coetzee T, Herschlag D, Belfort M. 1994. Escherichia coli proteins, including ribosomal protein S12, facilitate in vitro splicing of phage T4 introns by acting as RNA chaperones. Genes & Dev 8:1575-1588.
    • (1994) Genes & Dev , vol.8 , pp. 1575-1588
    • Coetzee, T.1    Herschlag, D.2    Belfort, M.3
  • 18
    • 0015497450 scopus 로고
    • Conformational changes of transfer ribonucleic acid. Equilibrium phase diagram
    • Cole PE, Yang SK, Crothers DM. 1972. Conformational changes of transfer ribonucleic acid. Equilibrium phase diagram. Biochemistry 11:4358-4368.
    • (1972) Biochemistry , vol.11 , pp. 4358-4368
    • Cole, P.E.1    Yang, S.K.2    Crothers, D.M.3
  • 19
    • 0032566329 scopus 로고    scopus 로고
    • A functional ribosomal RNA tertiary structure involves a base triple interaction
    • Conn GL, Gutell RR, Draper DE. 1998. A functional ribosomal RNA tertiary structure involves a base triple interaction. Biochemistry 37:11980-11988.
    • (1998) Biochemistry , vol.37 , pp. 11980-11988
    • Conn, G.L.1    Gutell, R.R.2    Draper, D.E.3
  • 20
    • 0031662075 scopus 로고    scopus 로고
    • Differential chemical probing of a group II self-splicing intron identifies bases involved in tertiary interactions and supports an alternative secondary structure model of domain V
    • Costa M, Christian EL, Michel F. 1998. Differential chemical probing of a group II self-splicing intron identifies bases involved in tertiary interactions and supports an alternative secondary structure model of domain V. RNA 4:1055-1068.
    • (1998) RNA , vol.4 , pp. 1055-1068
    • Costa, M.1    Christian, E.L.2    Michel, F.3
  • 21
    • 0028921811 scopus 로고
    • Frequent use of the same tertiary motif by self-folding RNAs
    • Costa M, Michel F. 1995. Frequent use of the same tertiary motif by self-folding RNAs. EMBO J 14:1276-1285.
    • (1995) EMBO J , vol.14 , pp. 1276-1285
    • Costa, M.1    Michel, F.2
  • 22
    • 0016169138 scopus 로고
    • The molecular mechanism of thermal unfolding of Escherichia coli formylmethionine transfer RNA
    • Crothers DM, Cole PE, Hilbers CW, Shulman RG. 1974. The molecular mechanism of thermal unfolding of Escherichia coli formylmethionine transfer RNA. J Mol Biol 87:63-88.
    • (1974) J Mol Biol , vol.87 , pp. 63-88
    • Crothers, D.M.1    Cole, P.E.2    Hilbers, C.W.3    Shulman, R.G.4
  • 23
    • 0028146967 scopus 로고
    • A comparative database of group I intron structures
    • Damberger SH, Gutell RR. 1994. A comparative database of group I intron structures. Nucleic Acids Res 22:3508-3510.
    • (1994) Nucleic Acids Res , vol.22 , pp. 3508-3510
    • Damberger, S.H.1    Gutell, R.R.2
  • 24
    • 0029877099 scopus 로고    scopus 로고
    • Parallel worlds
    • Draper DE. 1996. Parallel worlds. Nat Struct Biol 3:397-400.
    • (1996) Nat Struct Biol , vol.3 , pp. 397-400
    • Draper, D.E.1
  • 25
    • 0025238781 scopus 로고
    • Deletion-tolerance and trans-splicing of the bacteriophage T4 td intron
    • Galloway-Salvo JL, Coetzee T, Belfort M. 1990. Deletion-tolerance and trans-splicing of the bacteriophage T4 td intron. J Mol Biol 211:537-549.
    • (1990) J Mol Biol , vol.211 , pp. 537-549
    • Galloway-Salvo, J.L.1    Coetzee, T.2    Belfort, M.3
  • 26
    • 0028823370 scopus 로고
    • An interactive framework for RNA secondary structure prediction with a dynamical treatment of constraints
    • Gaspin C, Westhof E. 1995. An interactive framework for RNA secondary structure prediction with a dynamical treatment of constraints. J Mol Biol 254:163-174.
    • (1995) J Mol Biol , vol.254 , pp. 163-174
    • Gaspin, C.1    Westhof, E.2
  • 27
    • 0032500731 scopus 로고    scopus 로고
    • A preorganized active site in the crystal structure of the Tetrahymena ribozyme
    • Golden BL, Gooding AR, Podell ER, Cech TR. 1998. A preorganized active site in the crystal structure of the Tetrahymena ribozyme. Science 282:259-264.
    • (1998) Science , vol.282 , pp. 259-264
    • Golden, B.L.1    Gooding, A.R.2    Podell, E.R.3    Cech, T.R.4
  • 28
    • 0027433710 scopus 로고
    • Monitoring of the cooperative unfolding of the sun Y group I intron of bacteriophage T4
    • Jaeger L, Michel F, Westhof E. 1993. Monitoring of the cooperative unfolding of the sun Y group I intron of bacteriophage T4. J Mol Biol 234:331-346.
    • (1993) J Mol Biol , vol.234 , pp. 331-346
    • Jaeger, L.1    Michel, F.2    Westhof, E.3
  • 29
    • 0028294458 scopus 로고
    • Involvement of a GNRA tetraloop in long-range RNA tertiary interactions
    • Jaeger L, Michel F, Westhof E. 1994. Involvement of a GNRA tetraloop in long-range RNA tertiary interactions. J Mol Biol 236:1271-1276.
    • (1994) J Mol Biol , vol.236 , pp. 1271-1276
    • Jaeger, L.1    Michel, F.2    Westhof, E.3
  • 30
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel TA, Roberts JD, Zakour RA. 1987. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol 154:367-382.
    • (1987) Methods Enzymol , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 31
    • 0028234517 scopus 로고
    • Thermodynamics of RNA folding in a conserved ribosomal RNA domain
    • Laing LG, Draper DE. 1994. Thermodynamics of RNA folding in a conserved ribosomal RNA domain. J Mol Biol 237:560-576.
    • (1994) J Mol Biol , vol.237 , pp. 560-576
    • Laing, L.G.1    Draper, D.E.2
  • 32
    • 0027525989 scopus 로고
    • Evolution in vitro of an RNA enzyme with alteredmetal dependence
    • Lehman N, Joyce GF. 1993. Evolution in vitro of an RNA enzyme with alteredmetal dependence. Nature 361:182-185.
    • (1993) Nature , vol.361 , pp. 182-185
    • Lehman, N.1    Joyce, G.F.2
  • 33
    • 0030452773 scopus 로고    scopus 로고
    • New loop-loop tertiary interactions in self-splicing introns of subgroup IC and ID: A complete 3D model of the Tetrahymena thermophila ribozyme
    • Lehnert V, Jaeger L, Michel F, Westhof E. 1996. New loop-loop tertiary interactions in self-splicing introns of subgroup IC and ID: A complete 3D model of the Tetrahymena thermophila ribozyme. Chem Biol 3:993-1009.
    • (1996) Chem Biol , vol.3 , pp. 993-1009
    • Lehnert, V.1    Jaeger, L.2    Michel, F.3    Westhof, E.4
  • 34
    • 0032582795 scopus 로고    scopus 로고
    • Common motif organises the structure of multi-helix loop in 16S and 23S ribosomal RNAs
    • Leontis NB, Westhof E. 1998. Common motif organises the structure of multi-helix loop in 16S and 23S ribosomal RNAs. J Mol Biol 283:571-583.
    • (1998) J Mol Biol , vol.283 , pp. 571-583
    • Leontis, N.B.1    Westhof, E.2
  • 35
    • 0028316745 scopus 로고
    • Automatic identification of group I intron cores in genomic DNA sequences
    • Lisacek F, Diaz Y, Michel F. 1994. Automatic identification of group I intron cores in genomic DNA sequences. J Mol Biol 235:1206-1217.
    • (1994) J Mol Biol , vol.235 , pp. 1206-1217
    • Lisacek, F.1    Diaz, Y.2    Michel, F.3
  • 36
    • 0014429667 scopus 로고
    • Magnesium and the growth of Escherichia coli
    • Lusk JE, Williams RJP, Kennedy EP. 1968. Magnesium and the growth of Escherichia coli. J Biol Chem 243:2618-2624.
    • (1968) J Biol Chem , vol.243 , pp. 2618-2624
    • Lusk, J.E.1    Williams, R.J.P.2    Kennedy, E.P.3
  • 37
    • 0026770256 scopus 로고
    • Activation of the catalytic core of a group I intron by a remote 3′ splice junction
    • Michel F, Jaeger L, Westhof E, Kuras R, Tihy F, Xu M-Q, Shub DA. 1992. Activation of the catalytic core of a group I intron by a remote 3′ splice junction. Genes & Dev 6:1373-1385.
    • (1992) Genes & Dev , vol.6 , pp. 1373-1385
    • Michel, F.1    Jaeger, L.2    Westhof, E.3    Kuras, R.4    Tihy, F.5    Xu, M.-Q.6    Shub, D.A.7
  • 38
    • 0025678737 scopus 로고
    • Modelling of the three-dimensional architecture of group I catalytic introns based on comparative sequence analysis
    • Michel F, Westhof E. 1990. Modelling of the three-dimensional architecture of group I catalytic introns based on comparative sequence analysis. J Mol Biol 216:585-610.
    • (1990) J Mol Biol , vol.216 , pp. 585-610
    • Michel, F.1    Westhof, E.2
  • 39
    • 0026639175 scopus 로고
    • The Neurospora CYT-18 protein suppresses defects in the phage T4 td intron by stabilizing the catalytically active structure of the intron core
    • Mohr G, Zhang A, Gianelos JA, Belfort M, Lambowitz AM. 1992. The Neurospora CYT-18 protein suppresses defects in the phage T4 td intron by stabilizing the catalytically active structure of the intron core. Cell 69:483-494.
    • (1992) Cell , vol.69 , pp. 483-494
    • Mohr, G.1    Zhang, A.2    Gianelos, J.A.3    Belfort, M.4    Lambowitz, A.M.5
  • 40
    • 0030595381 scopus 로고    scopus 로고
    • A tyrosyl-tRNA synthetase suppresses structural defects in the two major helical domains of the group I intron catalytic core
    • Myers CA, Wallweber GJ, Rennard R, Kernel Y, Caprara MG, Mohr G, Lambowitz AM. 1996. A tyrosyl-tRNA synthetase suppresses structural defects in the two major helical domains of the group I intron catalytic core. J Mol Biol 262:87-104.
    • (1996) J Mol Biol , vol.262 , pp. 87-104
    • Myers, C.A.1    Wallweber, G.J.2    Rennard, R.3    Kernel, Y.4    Caprara, M.G.5    Mohr, G.6    Lambowitz, A.M.7
  • 41
    • 0021832962 scopus 로고
    • mRNA splicing efficiency in yeast and the contribution of nonconserved sequences
    • Pikielny CW, Rosbach M. 1985. mRNA splicing efficiency in yeast and the contribution of nonconserved sequences. Cell 41:119-126.
    • (1985) Cell , vol.41 , pp. 119-126
    • Pikielny, C.W.1    Rosbach, M.2
  • 42
    • 0031552363 scopus 로고    scopus 로고
    • Suppressors of cis-acting splicing-deficient mutations that affect the ribozyme core of a group II intron
    • Robineau S, Bergantino E, Carignani G, Michel F, Netter P. 1997. Suppressors of cis-acting splicing-deficient mutations that affect the ribozyme core of a group II intron. J Mol Biol 267:537-547.
    • (1997) J Mol Biol , vol.267 , pp. 537-547
    • Robineau, S.1    Bergantino, E.2    Carignani, G.3    Michel, F.4    Netter, P.5
  • 43
    • 0025828645 scopus 로고
    • Effects of mutations of the bulged nucleotide in the conserved P7 pairing element of the phage T4 td intron on ribozyme function
    • Schroeder R, von Ahsen U, Belfort M. 1991. Effects of mutations of the bulged nucleotide in the conserved P7 pairing element of the phage T4 td intron on ribozyme function. Biochemistry 30:3295-33303.
    • (1991) Biochemistry , vol.30 , pp. 3295-33303
    • Schroeder, R.1    Von Ahsen, U.2    Belfort, M.3
  • 44
    • 0032079494 scopus 로고    scopus 로고
    • A ribosomal function is necessary for efficient splicing of the T4 phage thymidylate synthase intron in vivo
    • Semrad K, Schroeder R. 1998. A ribosomal function is necessary for efficient splicing of the T4 phage thymidylate synthase intron in vivo. Genes & Dev 12:1327-1337.
    • (1998) Genes & Dev , vol.12 , pp. 1327-1337
    • Semrad, K.1    Schroeder, R.2
  • 46
    • 0024241761 scopus 로고
    • Structural analysis of RNA using chemical and enzymatic probing monitored by primer extension
    • Stern S, Moazed D, Noller HF. 1988. Structural analysis of RNA using chemical and enzymatic probing monitored by primer extension. Methods Enzymol 164:481-489.
    • (1988) Methods Enzymol , vol.164 , pp. 481-489
    • Stern, S.1    Moazed, D.2    Noller, H.F.3
  • 47
    • 0029985347 scopus 로고    scopus 로고
    • The environment of two metal ions surrounding the splice site of a group I intron
    • Streicher B, Westhof E, Schroeder R. 1996. The environment of two metal ions surrounding the splice site of a group I intron. EMBO J 15:2556-2564.
    • (1996) EMBO J , vol.15 , pp. 2556-2564
    • Streicher, B.1    Westhof, E.2    Schroeder, R.3
  • 48
    • 0031984645 scopus 로고    scopus 로고
    • Complementary sets of noncanonical base pairs mediate RNA helix packing in the group I intron active site
    • Strobel SA, Ortoleva-Donnelly L, Ryder SP, Cate JH, Moncoeur E. 1998. Complementary sets of noncanonical base pairs mediate RNA helix packing in the group I intron active site. Nat Struct Biol 5:60-65.
    • (1998) Nat Struct Biol , vol.5 , pp. 60-65
    • Strobel, S.A.1    Ortoleva-Donnelly, L.2    Ryder, S.P.3    Cate, J.H.4    Moncoeur, E.5
  • 49
    • 0030866522 scopus 로고    scopus 로고
    • Mutagenesis and comparative sequence analysis of a base triple joining the two domains of a group I ribozyme
    • Tanner MA, Anderson EM, Gutell RR, Cech TR. 1997. Mutagenesis and comparative sequence analysis of a base triple joining the two domains of a group I ribozyme. RNA 3:1037-1051.
    • (1997) RNA , vol.3 , pp. 1037-1051
    • Tanner, M.A.1    Anderson, E.M.2    Gutell, R.R.3    Cech, T.R.4
  • 50
    • 0027991626 scopus 로고
    • Kinetic intermediates in RNA folding
    • Zarrinkar PP, Williamson JR. 1994. Kinetic intermediates in RNA folding. Science 265:918-924.
    • (1994) Science , vol.265 , pp. 918-924
    • Zarrinkar, P.P.1    Williamson, J.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.