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Volumn 7, Issue 3, 1997, Pages 336-342

Protein-facilitated RNA folding

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; RIBONUCLEOPROTEIN; RNA; RNA BINDING PROTEIN;

EID: 0030916948     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(97)80048-6     Document Type: Article
Times cited : (110)

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    • Analysis of the CYT-18 protein binding site at the junction of stacked helices in a group I intron RNA by quantitative binding assays and in vitro selection
    • The CYT-18 splicing factor binds at the diffusion-controlled limit to a variety of group I intron deletion mutants as long as they include the P4-P6 triple-helical junction. Equilibrium binding affinities vary, however, which suggests that additional interactions are realized after the protein binds to the P4-P6 structure. A complex site spanning ten invariant residues is important for mediating specific complex formation. of outstanding interest
    • Saldanha R, Ellington A, Lambowitz AM. Analysis of the CYT-18 protein binding site at the junction of stacked helices in a group I intron RNA by quantitative binding assays and in vitro selection. J Mol Biol. 261:1996;23-42 The CYT-18 splicing factor binds at the diffusion-controlled limit to a variety of group I intron deletion mutants as long as they include the P4-P6 triple-helical junction. Equilibrium binding affinities vary, however, which suggests that additional interactions are realized after the protein binds to the P4-P6 structure. A complex site spanning ten invariant residues is important for mediating specific complex formation. of outstanding interest.
    • (1996) J Mol Biol , vol.261 , pp. 23-42
    • Saldanha, R.1    Ellington, A.2    Lambowitz, A.M.3
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    • The Cbp2 protein suppresses splice site mutations in a group I intron
    • Shaw LC, Thomas J Jr, Lewin AS. The Cbp2 protein suppresses splice site mutations in a group I intron. Nucleic Acids Res. 24:1996;3415-3423.
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    • Shaw, L.C.1    Thomas J., Jr.2    Lewin, A.S.3
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    • Kinetic and thermodynamic analysis of RNA - protein interactions in the RNase P holoenzyme from Escherichia coli
    • Talbot SJ, Altman S. Kinetic and thermodynamic analysis of RNA - protein interactions in the RNase P holoenzyme from Escherichia coli. Biochemistry. 33:1994;1406-1411.
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    • Talbot, S.J.1    Altman, S.2
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    • The DExH box protein Suv3p is a component of a yeast mitochondrial 3′- to-5' exoribonuclease that suppresses group I intron toxicity
    • The Suv3p protein, a DExH box helicase, is implicated in group I RNA degradation. The Suv3p-containing complex represents a neat way to recycle the protein components of group I intron-derived ribonucleoproteins. of outstanding interest
    • Margossian SP, Li H, Zassenhaus HP, Butow RA. The DExH box protein Suv3p is a component of a yeast mitochondrial 3′- to-5' exoribonuclease that suppresses group I intron toxicity. Cell. 84:1996;199-209 The Suv3p protein, a DExH box helicase, is implicated in group I RNA degradation. The Suv3p-containing complex represents a neat way to recycle the protein components of group I intron-derived ribonucleoproteins. of outstanding interest.
    • (1996) Cell , vol.84 , pp. 199-209
    • Margossian, S.P.1    Li, H.2    Zassenhaus, H.P.3    Butow, R.A.4
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    • Isolation and characterization of an NTP-dependent 3'-exoribonuclease from mitochondria of Saccharomyces cerevisiae
    • Min JJ, Heuertz RM, Zassenhaus HP. Isolation and characterization of an NTP-dependent 3'-exoribonuclease from mitochondria of Saccharomyces cerevisiae. J Biol Chem. 268:1993;7350-7357.
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    • Min, J.J.1    Heuertz, R.M.2    Zassenhaus, H.P.3
  • 50
    • 0030271457 scopus 로고    scopus 로고
    • RNA turnover and the control of mitochondrial gene expression
    • The authors thoughtfully review the problem of recycling the protein cofactors of group I introns. of special interest
    • Margossian SP, Butow RA. RNA turnover and the control of mitochondrial gene expression. Trends Biochem Sci. 21:1996;392-396 The authors thoughtfully review the problem of recycling the protein cofactors of group I introns. of special interest.
    • (1996) Trends Biochem Sci , vol.21 , pp. 392-396
    • Margossian, S.P.1    Butow, R.A.2
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    • An RNA topoisomerase
    • The authors find that E. coli DNA topoisomerase III possesses RNA topoi-somerase activity, raising the possibility that strand passage activities might contribute to RNA folding. of special interest
    • Wang H, Gate RJ, Seeman NC. An RNA topoisomerase. Proc Natl Acad Sci USA. 93:1996;9477-9482 The authors find that E. coli DNA topoisomerase III possesses RNA topoi-somerase activity, raising the possibility that strand passage activities might contribute to RNA folding. of special interest.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 9477-9482
    • Wang, H.1    Gate, R.J.2    Seeman, N.C.3
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    • A group II intron RNA is a catalytic component of a DNA endonuclease involved in intron mobility
    • In this and in a related paper [53], the authors show that the group II intron RNA al2 and its polyprotein cofactor collaborate to cleave double-stranded DNA. One DNA strand is cleaved by the RNA in a reverse splicing reaction, whereas the other strand is cleaved by one domain of the protein. A different domain of the protein enhances the RNA-splicing activity of the intron. Yet another domain of the protein possesses reverse transcriptase activity that contributes to intron mobility. of outstanding interest
    • Zimmerly S, Guo H, Eskes R, Yang J, Perlman PS, Lambowitz AM. A group II intron RNA is a catalytic component of a DNA endonuclease involved in intron mobility. Cell. 83:1995;529-538 In this and in a related paper [53], the authors show that the group II intron RNA al2 and its polyprotein cofactor collaborate to cleave double-stranded DNA. One DNA strand is cleaved by the RNA in a reverse splicing reaction, whereas the other strand is cleaved by one domain of the protein. A different domain of the protein enhances the RNA-splicing activity of the intron. Yet another domain of the protein possesses reverse transcriptase activity that contributes to intron mobility. of outstanding interest.
    • (1995) Cell , vol.83 , pp. 529-538
    • Zimmerly, S.1    Guo, H.2    Eskes, R.3    Yang, J.4    Perlman, P.S.5    Lambowitz, A.M.6
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    • Group II intron mobility occurs by target DNA-primed reverse transcription
    • See annotation [52]. of outstanding interest
    • Zimmerly S, Guo H, Perlman PS, Lambowitz AM. Group II intron mobility occurs by target DNA-primed reverse transcription. Cell. 82:1995;545-554 See annotation [52]. of outstanding interest.
    • (1995) Cell , vol.82 , pp. 545-554
    • Zimmerly, S.1    Guo, H.2    Perlman, P.S.3    Lambowitz, A.M.4
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    • The 'DEAD box' protein DbpA interacts specifically with the peptidyltransferase center in 23S rRNA
    • The RNA binding site for DbpA, a putative helicase and demonstrated RNA-dependent ATPase, is localized to a 93-nucleotide and functionally critical region of 16S RNA. of special interest
    • Nicol SM, Fuller-Pace FV. The 'DEAD box' protein DbpA interacts specifically with the peptidyltransferase center in 23S rRNA. Proc Natl Acad Sci USA. 92:1995;11681-11685 The RNA binding site for DbpA, a putative helicase and demonstrated RNA-dependent ATPase, is localized to a 93-nucleotide and functionally critical region of 16S RNA. of special interest.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 11681-11685
    • Nicol, S.M.1    Fuller-Pace, F.V.2
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    • 0029922992 scopus 로고    scopus 로고
    • A DEAD-box RNA helicase in the Escherichia coli RNA degradosome
    • The final stop for many RNAs is the degradosome - a complex that contains an essential ATP-dependent helicase. of special interest
    • Py B, Higgins CF, Krisch HM, Carpousis AJ. A DEAD-box RNA helicase in the Escherichia coli RNA degradosome. Nature. 381:1996;169-172 The final stop for many RNAs is the degradosome - a complex that contains an essential ATP-dependent helicase. of special interest.
    • (1996) Nature , vol.381 , pp. 169-172
    • Py, B.1    Higgins, C.F.2    Krisch, H.M.3    Carpousis, A.J.4
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    • Improved predictions of secondary structures for RNA
    • Jaeger JA, Turner DH, Zuker M. Improved predictions of secondary structures for RNA. Proc Natl Acad Sci USA. 86:1989;7706-7710.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 7706-7710
    • Jaeger, J.A.1    Turner, D.H.2    Zuker, M.3
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    • 0030582766 scopus 로고    scopus 로고
    • A tyrosyl-tRNA synthetase recognizes a conserved tRNA-like structural motif in the group I intron catalytic core
    • Tyr. Chemical footprinting and molecular modeling suggest CYT-18 recognizes overlapping structures that are centered at a stacked helix junction in both molecules. of special interest
    • Tyr. Chemical footprinting and molecular modeling suggest CYT-18 recognizes overlapping structures that are centered at a stacked helix junction in both molecules. of special interest.
    • (1996) Cell , vol.87 , pp. 1135-1145
    • Caprara, M.G.1    Lehnert, V.2    Lambowitz, A.M.3    Westhof, E.4
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    • 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 thermophilia ribozyme
    • The existence of good quality, medium resolution models for group I introns has been a boon to the ribozyme field. Models for group I RNAs belonging to four subgroups are now available and emphasize the modular organization of large RNAs. of special interest
    • Lehnert V, Jaeger L, Michel F, Westhof E. New loop - loop tertiary interactions in self-splicing introns of subgroup IC and ID: a complete 3D model of the Tetrahymena thermophilia ribozyme. Chem Biol. 3:1996;993-1009 The existence of good quality, medium resolution models for group I introns has been a boon to the ribozyme field. Models for group I RNAs belonging to four subgroups are now available and emphasize the modular organization of large RNAs. of special interest.
    • (1996) Chem Biol , vol.3 , pp. 993-1009
    • Lehnert, V.1    Jaeger, L.2    Michel, F.3    Westhof, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.