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Volumn 6, Issue 1, 1996, Pages 53-61

RNA-protein complexes

Author keywords

[No Author keywords available]

Indexed keywords

CAPSID PROTEIN; DOUBLE STRANDED RNA; MESSENGER RNA; RIBONUCLEOPROTEIN; RNA BINDING PROTEIN; RNA DIRECTED RNA POLYMERASE; SMALL NUCLEAR RNA;

EID: 0029913438     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(96)80095-9     Document Type: Article
Times cited : (160)

References (60)
  • 4
    • 0010550429 scopus 로고
    • Structure of RNA
    • Edited by Nagai K, Mattaj IW: Oxford: IRL Press
    • Varani G, Pardi A: Structure of RNA. In RNA-Protein Interactions. Edited by Nagai K, Mattaj IW: Oxford: IRL Press; 1994:1-24.
    • (1994) RNA-Protein Interactions , pp. 1-24
    • Varani, G.1    Pardi, A.2
  • 5
    • 0006163918 scopus 로고
    • RNA-protein interactions
    • Nagai K: RNA-protein interactions. Curr Opin Struct Biol 1992, 2:131-137.
    • (1992) Curr Opin Struct Biol , vol.2 , pp. 131-137
    • Nagai, K.1
  • 6
    • 0013364977 scopus 로고
    • Prediction and experimental investigation of RNA secondary and tertiary foldings
    • Edited by Nagai K, Mattaj IW. Oxford: IRL Press
    • Westhof E, Michel F: Prediction and experimental investigation of RNA secondary and tertiary foldings. In RNA-Protein Interactions. Edited by Nagai K, Mattaj IW. Oxford: IRL Press; 1994:25-51.
    • (1994) RNA-Protein Interactions , pp. 25-51
    • Westhof, E.1    Michel, F.2
  • 7
    • 0025744320 scopus 로고
    • Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase
    • Rould MA, Perona JJ, Steitz TA: Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase. Nature 1991, 352:213-218.
    • (1991) Nature , vol.352 , pp. 213-218
    • Rould, M.A.1    Perona, J.J.2    Steitz, T.A.3
  • 10
    • 0028004607 scopus 로고
    • Crystal structure at 1.92 a resolution of the RNA-binding domain of the U1a spliceosomal protein complexed with an RNA hairpin
    • Oubridge C, Ito N, Evans PR, Teo CH, Nagai K: Crystal structure at 1.92 A resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin. Nature 1994, 372:432-438. The crystal structure of a complex between U1A protein and hairpin II of U1snRNA was determined at 1.92 Å resolution. The AUUGCAC sequence within the 10-nucleotide loop interacts extensively with the RNP domain. The high-resolution structure allowed the determination of the precise stereochemistry of the RNA-protein contacts. Many direct and water-mediated hydrogen bonds are found at the protein-RNA interface.
    • (1994) Nature , vol.372 , pp. 432-438
    • Oubridge, C.1    Ito, N.2    Evans, P.R.3    Teo, C.H.4    Nagai, K.5
  • 11
    • 0027960331 scopus 로고
    • Crystal structure of an RNA bacteriophage coat protein-operator complex
    • Valegård K, Murray JB, Stockley PG, Storehouse NJ, Liljas L: Crystal structure of an RNA bacteriophage coat protein-operator complex. Nature 1994, 371:623-626. MS2 bacteriophage contains a single-stranded RNA genome and 180 copies of coat proteins assembled into a T=3 icosahedral surface lattice. A dimer of coat protein binds to a hairpin formed around the ribosomal binding site of the virally encoded replicase gene and initiates phage assembly. A 19-mer synthetic RNA was diffused into crystals of empty phage particles and its structure determined to 3.0 Å resolution.
    • (1994) Nature , vol.371 , pp. 623-626
    • Valegård, K.1    Murray, J.B.2    Stockley, P.G.3    Storehouse, N.J.4    Liljas, L.5
  • 12
    • 0027315727 scopus 로고
    • RNA recognition: A family matter
    • Mattaj IW: RNA recognition: a family matter. Cell 1993, 73:837-840.
    • (1993) Cell , vol.73 , pp. 837-840
    • Mattaj, I.W.1
  • 13
    • 0028129989 scopus 로고
    • Conserved structures and diversity of functions of RNA-binding proteins
    • Burd CG, Dreyfuss G: Conserved structures and diversity of functions of RNA-binding proteins. Science 1994, 265:615-621.
    • (1994) Science , vol.265 , pp. 615-621
    • Burd, C.G.1    Dreyfuss, G.2
  • 14
    • 0028990057 scopus 로고
    • The RNP domain: A sequence-specific RNA-binding domain involved in processing and transport of RNA
    • Nagai K, Oubridge C, Ito N, Avis J, Evans P: The RNP domain: a sequence-specific RNA-binding domain involved in processing and transport of RNA. Trends Biochem Sci 1995, 20:235-240. The RNP domain is the most commonly found RNA-binding domain. This review describes the architecture, evolution and RNA-binding properties of RNA-binding proteins in this family.
    • (1995) Trends Biochem Sci , vol.20 , pp. 235-240
    • Nagai, K.1    Oubridge, C.2    Ito, N.3    Avis, J.4    Evans, P.5
  • 15
    • 0029099218 scopus 로고
    • Eleven down and nine to go
    • Cusack S: Eleven down and nine to go. Nature Struct Biol 1995, 2:824-831. An excellent review discussing the architecture and evolution of aminoacyl-tRNA synthetases, which have modular structures. The conserved catalytic domain is combined with unrelated sequences which function as RNA-binding domains.
    • (1995) Nature Struct Biol , vol.2 , pp. 824-831
    • Cusack, S.1
  • 16
    • 0028964336 scopus 로고
    • The structure of trp RNA-binding attenuation protein
    • Antson AA, Otridge J, Brzozowski AM, Dodson EJ, Dodson GG, Wilson KS, Smith TM, Yang M, Kurecki T, Gollnick P: The structure of trp RNA-binding attenuation protein. Nature 1995, 374:693-700. The trp RNA-binding attenuation protein binds to the leader sequence of the tryptophan operon transcript, which contains 11 copies of the (U/G)AG triplets, causing termination of the transcription at high levels of tryptophan. The crystal structure of the protein complex with tryptophan determined at 1.8 Å resolution shows a novel structure containing 11 copies of monomers assembled into a doughnut-shaped ring. The structure suggests how this protein binds to the trp leader sequence in a manner dependent on tryptophan concentration.
    • (1995) Nature , vol.374 , pp. 693-700
    • Antson, A.A.1    Otridge, J.2    Brzozowski, A.M.3    Dodson, E.J.4    Dodson, G.G.5    Wilson, K.S.6    Smith, T.M.7    Yang, M.8    Kurecki, T.9    Gollnick, P.10
  • 17
    • 0024655246 scopus 로고
    • RNA-binding proteins as developmental regulators
    • Bandziulis RJ, Swanson MS, Dreyfuss G: RNA-binding proteins as developmental regulators. Genes Dev 1989, 3:431-437.
    • (1989) Genes Dev , vol.3 , pp. 431-437
    • Bandziulis, R.J.1    Swanson, M.S.2    Dreyfuss, G.3
  • 18
    • 0027753933 scopus 로고
    • Analysis of the RNA-recognition motif and RS and RGG domain: Conservation in metazoan pre-mRNA splicing factors
    • Birney E, Kumar S, Krainer AR: Analysis of the RNA-recognition motif and RS and RGG domain: conservation in metazoan pre-mRNA splicing factors. Nucleic Acids Res 1993, 21:5803-5816.
    • (1993) Nucleic Acids Res , vol.21 , pp. 5803-5816
    • Birney, E.1    Kumar, S.2    Krainer, A.R.3
  • 19
    • 0025221731 scopus 로고
    • Crystal structure of the RNA-binding domain of the U1 small nuclear ribonucleoprotein A
    • Nagai K, Oubridge C, Jessen TH, Li J, Evans PR: Crystal structure of the RNA-binding domain of the U1 small nuclear ribonucleoprotein A. Nature 1990, 348:515-520.
    • (1990) Nature , vol.348 , pp. 515-520
    • Nagai, K.1    Oubridge, C.2    Jessen, T.H.3    Li, J.4    Evans, P.R.5
  • 20
    • 0025964204 scopus 로고
    • RNA-binding domain of the a protein component of the U1 small nuclear ribonucleoprotein analyzed by NMR spectroscopy is structurally similar to ribosomal proteins
    • Hoffman DW, Query CC, Golden BL, White SW, Keene JD: RNA-binding domain of the A protein component of the U1 small nuclear ribonucleoprotein analyzed by NMR spectroscopy is structurally similar to ribosomal proteins. Proc Natl Acad Sci USA 1991, 88:2495-2499.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 2495-2499
    • Hoffman, D.W.1    Query, C.C.2    Golden, B.L.3    White, S.W.4    Keene, J.D.5
  • 21
    • 0028176929 scopus 로고
    • Determination of the secondary structure and folding topology of an RNA binding domain of mammalian hnRNP A1 protein using three-dimensional heteronuclear magnetic resonance spectroscopy
    • Garrett DS, Lodi PJ, Shamoo Y, Williams KR, Clore GM, Gronenborn AM: Determination of the secondary structure and folding topology of an RNA binding domain of mammalian hnRNP A1 protein using three-dimensional heteronuclear magnetic resonance spectroscopy. Biochemistry 1994, 33:2852-2858.
    • (1994) Biochemistry , vol.33 , pp. 2852-2858
    • Garrett, D.S.1    Lodi, P.J.2    Shamoo, Y.3    Williams, K.R.4    Clore, G.M.5    Gronenborn, A.M.6
  • 22
    • 0028965970 scopus 로고
    • An RBD that does not bind RNA: NMR secondary structure determinination and biochemical properties of the C-terminal RNA binding domain from the human U1A protein
    • Lu J, Hall KB: An RBD that does not bind RNA: NMR secondary structure determinination and biochemical properties of the C-terminal RNA binding domain from the human U1A protein. J Mol. Biol 1995, 247:739-752.
    • (1995) J Mol. Biol , vol.247 , pp. 739-752
    • Lu, J.1    Hall, K.B.2
  • 23
    • 0028027496 scopus 로고
    • Resonance assignments and solution structure of the 2nd RNA-binding domain of sex-lethal determined by multidimensional heteronuclear magnetic-resonance
    • Lee AL, Kanaar R, Rio DC, Wemmer DE: Resonance assignments and solution structure of the 2nd RNA-binding domain of sex-lethal determined by multidimensional heteronuclear magnetic-resonance. Biochemistry 1994, 33:13775-13786.
    • (1994) Biochemistry , vol.33 , pp. 13775-13786
    • Lee, A.L.1    Kanaar, R.2    Rio, D.C.3    Wemmer, D.E.4
  • 25
    • 0029978824 scopus 로고    scopus 로고
    • Solution structure of the N-terminal RNP domain of U1A protein: The role of C-terminal residues in structure stability and RNA binding
    • in press
    • Avis JM, Allain FHT, Howe P, Varani G, Nagai K, Neuhaus D: Solution structure of the N-terminal RNP domain of U1A protein: the role of C-terminal residues in structure stability and RNA binding. J Mol Biol 1996, in press.
    • (1996) J Mol Biol
    • Avis, J.M.1    Allain, F.H.T.2    Howe, P.3    Varani, G.4    Nagai, K.5    Neuhaus, D.6
  • 26
    • 0024851833 scopus 로고
    • Identification of the RNA-binding segment of human U1 A-protein and definition of its binding-site on U1 snRNA
    • Scherly D, Boelens W, Van Venrooij WJ, Dathan NA, Hamm J, Mattaj IW: Identification of the RNA-binding segment of human U1 A-protein and definition of its binding-site on U1 snRNA. EMBO J 1989, 8:4163-4170.
    • (1989) EMBO J , vol.8 , pp. 4163-4170
    • Scherly, D.1    Boelens, W.2    Van Venrooij, W.J.3    Dathan, N.A.4    Hamm, J.5    Mattaj, I.W.6
  • 27
    • 0025938601 scopus 로고
    • Identification of molecular contacts between the U1A small nuclear ribonucleoprotein and U1 RNA
    • Jessen TH, Oubridge CJ, Teo CH, Prichard C, Nagai K: Identification of molecular contacts between the U1A small nuclear ribonucleoprotein and U1 RNA. EMBO J 1991, 10:3447-3456.
    • (1991) EMBO J , vol.10 , pp. 3447-3456
    • Jessen, T.H.1    Oubridge, C.J.2    Teo, C.H.3    Prichard, C.4    Nagai, K.5
  • 28
    • 0027105279 scopus 로고
    • Two RNA-binding motifs in the double-stranded RNA-activated protein kinase DAI
    • Green SR, Mathews M: Two RNA-binding motifs in the double-stranded RNA-activated protein kinase DAI. Genes Dev 1992, 6:2478-2490.
    • (1992) Genes Dev , vol.6 , pp. 2478-2490
    • Green, S.R.1    Mathews, M.2
  • 30
    • 0028285542 scopus 로고
    • Detection of dsRNA-binding domains in RNA helicase a and Drosophila maleless: Implications for monomeric RNA helicases
    • Gibson TJ, Thompson JD: Detection of dsRNA-binding domains in RNA helicase A and Drosophila maleless: implications for monomeric RNA helicases. Nucleic Acids Res 1994, 22:2552-2556. A sequence database search with dsRBD profiles detected more proteins in this family. These include RNA helicase A containing two dsRBDs and a helicase domain (containing a DEAD/DExH box).
    • (1994) Nucleic Acids Res , vol.22 , pp. 2552-2556
    • Gibson, T.J.1    Thompson, J.D.2
  • 31
    • 0028639195 scopus 로고
    • Staufen protein associates with the 3′UTR of bicoid mRNa to form particles which move in a microtubule-dependent manner
    • Ferrandon D, Elphick L, Nüsslein-Volhard C, St Johnston D: Staufen protein associates with the 3′UTR of bicoid mRNA to form particles which move in a microtubule-dependent manner. Cell 1994, 79:1221-1231. The Drosophila staufen protein is involved in the localization of maternal mRNA such as bicoid and oskar and thereby plays a crucial role in the formation of body pattern. Staufen protein contains five copies of dsRBD and interacts with the 400 nucledotide 3′ UTR of bicoid mRNA.
    • (1994) Cell , vol.79 , pp. 1221-1231
    • Ferrandon, D.1    Elphick, L.2    Nüsslein-Volhard, C.3    St Johnston, D.4
  • 32
    • 0025885105 scopus 로고
    • Staufen, a gene required to localise maternal RNAs in the Drosophila egg
    • St Johnston D, Beuchle D, Nüsslein-Volhard C: Staufen, a gene required to localise maternal RNAs in the Drosophila egg. Cell 1991, 66:51-63.
    • (1991) Cell , vol.66 , pp. 51-63
    • St Johnston, D.1    Beuchle, D.2    Nüsslein-Volhard, C.3
  • 33
    • 0027105279 scopus 로고
    • Two RNA-binding motifs in the double-stranded RNA-activated protein kinase, DAI
    • Green SR, Mathew MB: Two RNA-binding motifs in the double-stranded RNA-activated protein kinase, DAI. Genes Dev 1992, 6:2478-2490.
    • (1992) Genes Dev , vol.6 , pp. 2478-2490
    • Green, S.R.1    Mathew, M.B.2
  • 34
    • 0028961190 scopus 로고
    • Two functionally distinct RNA-binding motifs in the regulatory domain of the protein kinase DAI
    • Green SR, Manche L, Mathews MB: Two functionally distinct RNA-binding motifs in the regulatory domain of the protein kinase DAI. Mol Cell Biol 1995, 15:358-364.
    • (1995) Mol Cell Biol , vol.15 , pp. 358-364
    • Green, S.R.1    Manche, L.2    Mathews, M.B.3
  • 35
    • 0027972952 scopus 로고
    • Molecular cloning of cDNa for double-stranded RNa adenosine deaminase, a candidate enyzme for nuclear RNa editing
    • Kim U, Wang Y, Sanford T, Zeng Y, Nishikura K: Molecular cloning of cDNA for double-stranded RNA adenosine deaminase, a candidate enyzme for nuclear RNA editing. Proc Natl Acad Sci USA 1994, 91:11457-11461. A cDNA clone for double-stranded RNA adenosine deaminase was obtained from a human natural killer cell cDNA library. This enzyme catalyzes the A→I conversion of double-stranded RNA and is thought to be involved in the editing of transcripts encoding glutamate-gated ion channels in the brain.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 11457-11461
    • Kim, U.1    Wang, Y.2    Sanford, T.3    Zeng, Y.4    Nishikura, K.5
  • 36
    • 0027967784 scopus 로고
    • Preferential selection of adenosines for modification by double-stranded RNA adenosine deaminase
    • Poison AG, Bass BL: Preferential selection of adenosines for modification by double-stranded RNA adenosine deaminase. EMBO J 1994, 13:5701 -5711. Enzymatic specificity of dsRNA adenosine deaminase was studied by RNase U2 and T1 mapping of modified substrate RNA. The modified adenosine has a 5′ but not 3′ neighbour preference. The results suggest that the specific editing of glutamate receptor mRNA could be carried out by this enzyme without the aid of specificity factors.
    • (1994) EMBO J , vol.13 , pp. 5701-5711
    • Poison, A.G.1    Bass, B.L.2
  • 37
    • 0029058994 scopus 로고
    • Structure of the dsRNA binding domain of E. coli RNase III
    • Kharrat A, Macias MJ, Gibson TJ, Nilges M, Pastore A: Structure of the dsRNA binding domain of E. coli RNase III. EMBO J 1995, 14:3572-3584. The structure of the dsRBD of E. coli RNase III was determined by NMR. It has a three-stranded β sheet packed against two α helices. Conserved positively charged residues found on the loops on one side of the molecule are implicated in RNA binding.
    • (1995) EMBO J , vol.14 , pp. 3572-3584
    • Kharrat, A.1    Macias, M.J.2    Gibson, T.J.3    Nilges, M.4    Pastore, A.5
  • 38
    • 0029041105 scopus 로고
    • NMR solution structure of a dsRNa binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5
    • Bycroft M, Grünert S, Murzin AG, Proctor M, St Johnston D: NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5. EMBO J 1995, 14:3563-3571. The structure of one of the dsRBDs from Drosophila staufen protein has been determined by NMR. It has a three-stranded ß sheet flanked on one side by two α helices. The protein has remarkable sequence and structural similarity to the N-terminal domain of ribosomal protein S5. The RNA-binding residues identified by mutagenesis experiments are located on the loops on one side of the molecule.
    • (1995) EMBO J , vol.14 , pp. 3563-3571
    • Bycroft, M.1    Grünert, S.2    Murzin, A.G.3    Proctor, M.4    St Johnston, D.5
  • 39
    • 0027273728 scopus 로고
    • The pre-mRNa binding K protein contains a novel evolutionarily conserved motif
    • Siomi H, Matunis MJ, Michael WM, Dreyfuss G: The pre-mRNA binding K protein contains a novel evolutionarily conserved motif. Nucleic Acids Res 1993, 21:1193-1198.
    • (1993) Nucleic Acids Res , vol.21 , pp. 1193-1198
    • Siomi, H.1    Matunis, M.J.2    Michael, W.M.3    Dreyfuss, G.4
  • 40
    • 0027258576 scopus 로고
    • The KH domain occurs in a diverse set of RNA-binding proteins that include the antiterminator NusA and is probably involved in binding to nucleic acid
    • Gibson TJ, Tompson JD, Herringa J: The KH domain occurs in a diverse set of RNA-binding proteins that include the antiterminator NusA and is probably involved in binding to nucleic acid. FEBS Lett 1993, 324:361-366.
    • (1993) FEBS Lett , vol.324 , pp. 361-366
    • Gibson, T.J.1    Tompson, J.D.2    Herringa, J.3
  • 42
    • 0028236525 scopus 로고
    • Essential role for KH domains in RNA binding: Impaired RNA binding by a mutation in the KH domain of FMR1 that causes fragile X syndrome
    • Siomi H, Choi M, Siomi MC, Nussbaum RL, Dreyfuss G: Essential role for KH domains in RNA binding: impaired RNA binding by a mutation in the KH domain of FMR1 that causes fragile X syndrome. Cell 1994, 77:33-39. RNA-binding properties of hnRNP protein K were studied by mutagenesis. The conserved residues of all three KH domains of this protein are required for the wild-type RNA-binding activities. The lle304Asn mutation in one of the KH domains of the fragile X mental retardation gene product is known to cause hereditary mental retardation. The in vitro RNA-binding activity of this protein is severely impaired by the lle304Asn mutation.
    • (1994) Cell , vol.77 , pp. 33-39
    • Siomi, H.1    Choi, M.2    Siomi, M.C.3    Nussbaum, R.L.4    Dreyfuss, G.5
  • 43
    • 0029125496 scopus 로고
    • Identification of two KH domain proteins in the α-globin mRNP stability complex
    • Kiledjian M, Wang X, Liebhaber SA: Identification of two KH domain proteins in the α-globin mRNP stability complex. EMBO J 1995, 14:4357-4364. The cDNAs for two proteins associated with α-globin mRNA have been cloned. These proteins are part of α-globin mRNP, which stabilizes α-globin mRNA in vivo.
    • (1995) EMBO J , vol.14 , pp. 4357-4364
    • Kiledjian, M.1    Wang, X.2    Liebhaber, S.A.3
  • 44
    • 0028798720 scopus 로고
    • The KH module has an αβ fold
    • Morelli MAC, Stier G, Gibson T, Joseph C, Musco G, Pastore A, Travè G: The KH module has an αβ fold. FEBS Lett 1995, 358:193-198. The structure of the KH domain from human vigilin was studied by multidimensional NMR. This domain has a β-α-α-β-β-α topology.
    • (1995) FEBS Lett , vol.358 , pp. 193-198
    • Morelli, M.A.C.1    Stier, G.2    Gibson, T.3    Joseph, C.4    Musco, G.5    Pastore, A.6    Travè, G.7
  • 45
    • 0029054375 scopus 로고
    • Identification and characterization of Uss1p (Sdb23p): A novel U6 snRNA-associated protein with significant similarity to core proteins of small nuclear ribonucleoproteins
    • Cooper M, Johnston LH, Beggs JD: Identification and characterization of Uss1p (Sdb23p): a novel U6 snRNA-associated protein with significant similarity to core proteins of small nuclear ribonucleoproteins. EMBO J 1995, 14:2066-2075. The SDB23 gene of Saccharomyces cerevisiae was originally isolated as a suppressor of mutation in a cell cycle gene, DBF2. This paper shows that the SDB23 gene product is associated with U6 snRNA and hence it is essential for nuclear pre-mRNA splicing and cell viability. The authors therefore propose the more logical name USS1 (U-six snRNP) for this gene. The multiple sequence alignment of snRNP core proteins with USS1 led to the discovery of a common sequence motif in the core Sm proteins.
    • (1995) EMBO J , vol.14 , pp. 2066-2075
    • Cooper, M.1    Johnston, L.H.2    Beggs, J.D.3
  • 46
    • 0029054377 scopus 로고
    • snRNP Sm proteins share two evolutionary conserved sequence motifs which are involved in Sm protein-protein interactions
    • Hermann H, Fabrizio P, Raker VA, Foulaki K, Hornig H, Brahms H, Lührmann R: snRNP Sm proteins share two evolutionary conserved sequence motifs which are involved in Sm protein-protein interactions. EMBO J 1995, 14:2076-2088. Complementary DNA (cDNA) sequences for snRNP core proteins have been cloned on the basis of the partial protein sequences. An evolutionary conserved sequence motif, the Sm motif, was discovered by the alignment of these core protein sequences.
    • (1995) EMBO J , vol.14 , pp. 2076-2088
    • Hermann, H.1    Fabrizio, P.2    Raker, V.A.3    Foulaki, K.4    Hornig, H.5    Brahms, H.6    Lührmann, R.7
  • 47
    • 0028997105 scopus 로고
    • Sm and Sm-like proteins belong to a large family: Identification of proteins of the U6 as well as the U1, U2, U4 and US snRNPs
    • Séraphin B: Sm and Sm-like proteins belong to a large family: identification of proteins of the U6 as well as the U1, U2, U4 and US snRNPs. EMBO J 1995, 14:2089-2098. A common sequence motif was discovered among the core Sm-proteins by sequence alignment. Database searches using this motif uncovered a large number of Sm-like proteins from plants, animals and fungi.
    • (1995) EMBO J , vol.14 , pp. 2089-2098
    • Séraphin, B.1
  • 48
    • 0011220277 scopus 로고
    • Interaction of 5S RNA with TFIIIA
    • Edited by Nagai K, Mattaj IW: Oxford: IRL Press
    • Pieler T: Interaction of 5S RNA with TFIIIA. In RNA-Protein Interactions. Edited by Nagai K, Mattaj IW: Oxford: IRL Press; 1994:178-191.
    • (1994) RNA-Protein Interactions , pp. 178-191
    • Pieler, T.1
  • 49
    • 0023478466 scopus 로고
    • cDNa cloning of the human U1snRNA-associated A protein: Extensive homology between U1 and U2 snRNP-specific proteins
    • Sillekens PTG, Habets WJ, Beijer RP, Van Venrooij WJ: cDNA cloning of the human U1snRNA-associated A protein: extensive homology between U1 and U2 snRNP-specific proteins. EMBO J 1987, 6:3841-3848.
    • (1987) EMBO J , vol.6 , pp. 3841-3848
    • Sillekens, P.T.G.1    Habets, W.J.2    Beijer, R.P.3    Van Venrooij, W.J.4
  • 53
    • 0027140498 scopus 로고
    • The refined structure of bacteriophage MS2 at 2.8 Å resolution
    • Golmohammadi R, Valegård K, Fridborg K, Liljas L: The refined structure of bacteriophage MS2 at 2.8 Å resolution. J Mol Biol 1993, 234:620-639.
    • (1993) J Mol Biol , vol.234 , pp. 620-639
    • Golmohammadi, R.1    Valegård, K.2    Fridborg, K.3    Liljas, L.4
  • 54
    • 0029024877 scopus 로고
    • Proton NMR and structural features of a 24-nucleotide RNA hairpin
    • Borer PN, Lin Y, Wang S, Roggenbuck MW, Gott JM, Uhlenbeck OC, Pelczer I: Proton NMR and structural features of a 24-nucleotide RNA hairpin. Biochemistry 1995, 34:6488-6503. The structure of an RNA closely related to the target of MS2 phage has been investigated by NMR.
    • (1995) Biochemistry , vol.34 , pp. 6488-6503
    • Borer, P.N.1    Lin, Y.2    Wang, S.3    Roggenbuck, M.W.4    Gott, J.M.5    Uhlenbeck, O.C.6    Pelczer, I.7
  • 55
    • 0027518457 scopus 로고
    • Ordered duplex RNA controls capsid architecture in an icosahedral animal virus
    • Fisher AJ, Johnson JE: Ordered duplex RNA controls capsid architecture in an icosahedral animal virus. Nature 1993, 361:176-179.
    • (1993) Nature , vol.361 , pp. 176-179
    • Fisher, A.J.1    Johnson, J.E.2
  • 58
    • 0029035582 scopus 로고
    • Crystal structure of the T4 rega translational regulator protein at 1.9 a resolution
    • Kang CH, Chan R, Berger I, Lockshin C, Green L, Gold L, Rich A: Crystal structure of the T4 regA translational regulator protein at 1.9 A resolution. Science 1995, 268:1170-1173. T4 bacteriophage regA protein binds to many early T4 mRNAs near the ribosomal binding sites and diminishes translation. The crystal structure of T4 regA protein determined at 1.9 Å resolution has two antiparallel β sheets, one of which is implicated in RNA binding.
    • (1995) Science , vol.268 , pp. 1170-1173
    • Kang, C.H.1    Chan, R.2    Berger, I.3    Lockshin, C.4    Green, L.5    Gold, L.6    Rich, A.7
  • 59
    • 0028873824 scopus 로고
    • Dissecting RNA-protein interactions: RNA-RNA recognition by Rop
    • Predki PF, Nayak LM, Gottlieb MBC, Regan L: Dissecting RNA-protein interactions: RNA-RNA recognition by Rop. Cell 1995, 80:41-50. Rop protein encoded by CoIE1 plasmids is a small RNA-binding protein which facilitates pairing between two RNA hairpins within RNA I and complementary RNA II. Two molecules of Rop proteins form a four-helix bundle. Based on the crystal structure, surface residues were mutated and the RNA-binding properties of mutant proteins were studied.
    • (1995) Cell , vol.80 , pp. 41-50
    • Predki, P.F.1    Nayak, L.M.2    Gottlieb, M.B.C.3    Regan, L.4
  • 60
    • 0026244229 scopus 로고
    • MOLSCRIPT - A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ: MOLSCRIPT - a program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 1991, 24:946-950.
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.