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Volumn 272, Issue 1, 1997, Pages 82-94

A characteristic arrangement of aromatic amino acid residues in the solution structure of the amino-terminal RNA-binding domain of Drosophila sex-lethal

Author keywords

NMR; RNA binding domain; RNP motif; Sex lethal; Tertiary structure

Indexed keywords

MUTANT PROTEIN; RNA BINDING PROTEIN;

EID: 0031565722     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1213     Document Type: Article
Times cited : (23)

References (50)
  • 1
    • 0029967164 scopus 로고    scopus 로고
    • Target specificities of neuronal RNA-binding protein, Mel-N1: Direct binding to the 3′ untranslated region of its own mRNA
    • Abe R., Yamamoto K., Sakamoto H. Target specificities of neuronal RNA-binding protein, Mel-N1: direct binding to the 3′ untranslated region of its own mRNA. Nucl. Acids Res. 24:1996a;2011-2016.
    • (1996) Nucl. Acids Res. , vol.24 , pp. 2011-2016
    • Abe, R.1    Yamamoto, K.2    Sakamoto, H.3
  • 2
    • 0030459516 scopus 로고    scopus 로고
    • Two different RNA binding activities for the AU-rich element and the poly(A) sequence of the mouse neuronal protein mHuC
    • Abe R., Sakashita E., Yamamoto K., Sakamoto H. Two different RNA binding activities for the AU-rich element and the poly(A) sequence of the mouse neuronal protein mHuC. Nucl. Acids Res. 24:1996b;4895-4901.
    • (1996) Nucl. Acids Res. , vol.24 , pp. 4895-4901
    • Abe, R.1    Sakashita, E.2    Yamamoto, K.3    Sakamoto, H.4
  • 3
    • 0029920331 scopus 로고    scopus 로고
    • Specificity of ribonucleoprotein interaction determined by RNA folding during complex formulation
    • Allain F. H., Gubser C. C., Howe P. W., Nagai K., Neuhaus D., Varani G. Specificity of ribonucleoprotein interaction determined by RNA folding during complex formulation. Nature. 380:1996;646-650.
    • (1996) Nature , vol.380 , pp. 646-650
    • Allain, F.H.1    Gubser, C.C.2    Howe, P.W.3    Nagai, K.4    Neuhaus, D.5    Varani, G.6
  • 5
    • 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
    • Avis J. M., Allain F. H., Howe P. W., 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. 257:1996;398-411.
    • (1996) J. Mol. Biol. , vol.257 , pp. 398-411
    • Avis, J.M.1    Allain, F.H.2    Howe, P.W.3    Varani, G.4    Nagai, K.5    Neuhaus, D.6
  • 6
    • 0024328766 scopus 로고
    • Sex in flies: The splice of life
    • Baker B. S. Sex in flies: the splice of life. Nature. 340:1989;521-524.
    • (1989) Nature , vol.340 , pp. 521-524
    • Baker, B.S.1
  • 7
    • 0024655246 scopus 로고
    • RNA-binding proteins as developmental regulators
    • Bandziulis R. J., Swanson M. S., Dreyfuss G. RNA-binding proteins as developmental regulators. Genes Dev. 3:1989;431-437.
    • (1989) Genes Dev. , vol.3 , pp. 431-437
    • Bandziulis, R.J.1    Swanson, M.S.2    Dreyfuss, G.3
  • 8
    • 5144233105 scopus 로고
    • MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax A., Davis G. MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 65:1985;355-360.
    • (1985) J. Magn. Reson. , vol.65 , pp. 355-360
    • Bax, A.1    Davis, G.2
  • 10
    • 0027753933 scopus 로고
    • Analysis of the RNA-recognition motif and RS and RGG domains: Conservation in metazoan pre-mRNA splicing factors
    • Birney E., Kumar S., Krainer A. R. Analysis of the RNA-recognition motif and RS and RGG domains: conservation in metazoan pre-mRNA splicing factors. Nucl. Acids Res. 21:1993;5803-5816.
    • (1993) Nucl. Acids Res. , vol.21 , pp. 5803-5816
    • Birney, E.1    Kumar, S.2    Krainer, A.R.3
  • 11
    • 0011491177 scopus 로고
    • Structure determination of a tetrasaccharide: Transient nuclear Overhauser effects in the rotating frame
    • Bothner-By A. A., Stephans R. L., Lee J. -M., Warren C. D., Jeanloz R. W. Structure determination of a tetrasaccharide: Transient nuclear Overhauser effects in the rotating frame. J. Am. Chem. Soc. 106:1984;811-813.
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 811-813
    • Bothner-By, A.A.1    Stephans, R.L.2    Lee, J.-M.3    Warren, C.D.4    Jeanloz, R.W.5
  • 14
    • 0028129989 scopus 로고
    • Conserved structures and diversities of function of RNA binding proteins
    • Burd C. G., Dreyfuss G. Conserved structures and diversities of function of RNA binding proteins. Science. 265:1994;615-621.
    • (1994) Science , vol.265 , pp. 615-621
    • Burd, C.G.1    Dreyfuss, G.2
  • 15
    • 15844401767 scopus 로고    scopus 로고
    • Purification and properties of HuD, a neuronal RNA-binding protein
    • Chung S., Jiang L., Chung S., Furneaux H. Purification and properties of HuD, a neuronal RNA-binding protein. J. Biol. Chem. 271:1996;11518-11524.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11518-11524
    • Chung, S.1    Jiang, L.2    Chung, S.3    Furneaux, H.4
  • 16
    • 0023475020 scopus 로고
    • Three-dimensional structures of dotato carboxypeptidase inhibitor in solution. A study using nuclear magnetic resonance, distance geometry, and restrained molecular dynamics
    • Clore G. M., Gronenborn A. M., Nilges M., Ryan C. A. Three-dimensional structures of dotato carboxypeptidase inhibitor in solution. A study using nuclear magnetic resonance, distance geometry, and restrained molecular dynamics. Biochemistry. 26:1987;8012-8023.
    • (1987) Biochemistry , vol.26 , pp. 8012-8023
    • Clore, G.M.1    Gronenborn, A.M.2    Nilges, M.3    Ryan, C.A.4
  • 17
    • 0025772135 scopus 로고
    • High-resolution three-dimensional structure of interleukin 1β in solution by three- and four-dimensional nuclear magnetic resonance spectroscopy
    • Clore G. M., Wingfield P. T., Gronenborn A. M. High-resolution three-dimensional structure of interleukin 1β in solution by three- and four-dimensional nuclear magnetic resonance spectroscopy. Biochemistry. 30:1991;2315-2323.
    • (1991) Biochemistry , vol.30 , pp. 2315-2323
    • Clore, G.M.1    Wingfield, P.T.2    Gronenborn, A.M.3
  • 20
    • 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 D. S., Lodi P. J., Shamoo Y., Williams K. R., Clore G. M., Gronenborn A. M. 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. 33:1994;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
  • 21
    • 0001240703 scopus 로고
    • Frequency offset effects and their elimination in NMR rotating-frame cross-relaxation spectroscopy
    • Griesinger C., Ernst R. R. Frequency offset effects and their elimination in NMR rotating-frame cross-relaxation spectroscopy. J. Magn. Reson. 75:1987;261-271.
    • (1987) J. Magn. Reson. , vol.75 , pp. 261-271
    • Griesinger, C.1    Ernst, R.R.2
  • 22
    • 0025363553 scopus 로고
    • Binding of the Drosophila sex-lethal gene product to the alternative splice site of transformer primary transcript
    • Inoue K., Hoshijima K., Sakamoto H., Shimura Y. Binding of the Drosophila sex-lethal gene product to the alternative splice site of transformer primary transcript. Nature. 344:1990;461-463.
    • (1990) Nature , vol.344 , pp. 461-463
    • Inoue, K.1    Hoshijima, K.2    Sakamoto, H.3    Shimura, Y.4
  • 23
    • 0343359244 scopus 로고
    • Investigation of exchange process by two-dimensional NMR spectroscopy
    • Jeener J., Meier B. H., Bachmann P., Ernst R. R. Investigation of exchange process by two-dimensional NMR spectroscopy. J. Chem. Phys. 71:1979;4546-4553.
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 24
    • 0029115921 scopus 로고
    • Interaction of the sex-lethal RNA binding domains with RNA
    • Kanaar R., Lee A. L., Rudner D. Z., Wemmer D. E., Rio D. C. Interaction of the sex-lethal RNA binding domains with RNA. EMBO J. 14:1995;4530-4539.
    • (1995) EMBO J. , vol.14 , pp. 4530-4539
    • Kanaar, R.1    Lee, A.L.2    Rudner, D.Z.3    Wemmer, D.E.4    Rio, D.C.5
  • 26
    • 0025761656 scopus 로고
    • RNA recognition: Towards identifying determinants of specificity
    • Kenan D. J., Query C. C., Keene J. D. RNA recognition: towards identifying determinants of specificity. Trends Biochem. Sci. 16:1991;214-220.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 214-220
    • Kenan, D.J.1    Query, C.C.2    Keene, J.D.3
  • 27
    • 0029365773 scopus 로고
    • Cell-free synthesis and amino acid-selective stable isotope labeling of proteins for NMR analysis
    • Kigawa T., Muto Y., Yokoyama S. Cell-free synthesis and amino acid-selective stable isotope labeling of proteins for NMR analysis. J. Biomol. NMR. 6:1995;129-134.
    • (1995) J. Biomol. NMR , vol.6 , pp. 129-134
    • Kigawa, T.1    Muto, Y.2    Yokoyama, S.3
  • 28
    • 0027514572 scopus 로고
    • Isolation of RRM-type RNA-binding protein genes and the analysis of their relatedness by using a numerical approach
    • Kim Y. J., Baker B. S. Isolation of RRM-type RNA-binding protein genes and the analysis of their relatedness by using a numerical approach. Mol. Cell Biol. 13:1993;174-183.
    • (1993) Mol. Cell Biol. , vol.13 , pp. 174-183
    • Kim, Y.J.1    Baker, B.S.2
  • 30
    • 0028027496 scopus 로고
    • Resonance assignments and solution structure of the second RNA-binding domain of Sex-lethal determined by multidimensional heteronuclear magnetic resonance
    • Lee A. L., Kanaar R., Rio D. C., Wemmer D. E. Resonance assignments and solution structure of the second RNA-binding domain of Sex-lethal determined by multidimensional heteronuclear magnetic resonance. Biochemistry. 33:1994;13775-13786.
    • (1994) Biochemistry , vol.33 , pp. 13775-13786
    • Lee, A.L.1    Kanaar, R.2    Rio, D.C.3    Wemmer, D.E.4
  • 31
    • 0027314350 scopus 로고
    • Hel-N1: An autoimmune RNA-binding protein with specificity for 3′ uridylate-rich untranslated regions of growth factor mRNAs
    • Levine T. D., Gao F., King P. H., Andrews L. G., Keene J. D. Hel-N1: an autoimmune RNA-binding protein with specificity for 3′ uridylate-rich untranslated regions of growth factor mRNAs. Mol. Cell. Biol. 13:1993;3494-3504.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 3494-3504
    • Levine, T.D.1    Gao, F.2    King, P.H.3    Andrews, L.G.4    Keene, J.D.5
  • 32
    • 0029019508 scopus 로고
    • Paraneoplastic encephalomyelitis antigens bind to the AU-rich elements of mRNA
    • Liu J., Dalmau J., Szabo A., Rosenfeld M., Huber J., Furneaux H. Paraneoplastic encephalomyelitis antigens bind to the AU-rich elements of mRNA. Neurology. 45:1995;544-550.
    • (1995) Neurology , vol.45 , pp. 544-550
    • Liu, J.1    Dalmau, J.2    Szabo, A.3    Rosenfeld, M.4    Huber, J.5    Furneaux, H.6
  • 33
    • 0028965970 scopus 로고
    • An RBD that does not bind RNA: NMR secondary structure determination and biochemical properties of the C-terminal RNA binding domain from the human U1A protein
    • Lu J., Hall K. B. An RBD that does not bind RNA: NMR secondary structure determination and biochemical properties of the C-terminal RNA binding domain from the human U1A protein. J. Mol. Biol. 247:1995;739-752.
    • (1995) J. Mol. Biol. , vol.247 , pp. 739-752
    • Lu, J.1    Hall, K.B.2
  • 34
    • 0029873536 scopus 로고    scopus 로고
    • Cloning and characterization of HuR, a ubiquitously expressed Elav-like protein
    • Ma W., Cheng S., Campbell C., Wright A., Furneaux H. Cloning and characterization of HuR, a ubiquitously expressed Elav-like protein. J. Biol. Chem. 271:1996;8144-8151.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8144-8151
    • Ma, W.1    Cheng, S.2    Campbell, C.3    Wright, A.4    Furneaux, H.5
  • 35
    • 0025221731 scopus 로고
    • Crystal structure of the RNA-binding domain of the U1 small nuclear ribonucleoprotein A
    • Nagai K., Oubridge C., Jessen T., Li J., Evans P. R. Crystal structure of the RNA-binding domain of the U1 small nuclear ribonucleoprotein A. Nature. 348:1990;515-520.
    • (1990) Nature , vol.348 , pp. 515-520
    • Nagai, K.1    Oubridge, C.2    Jessen, T.3    Li, J.4    Evans, P.R.5
  • 37
    • 0023732144 scopus 로고
    • Determination of three-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms
    • Nilges M., Clore M., Gronenborn A. M. Determination of three-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms. FEBS Letters. 239:1991;129-136.
    • (1991) FEBS Letters , vol.239 , pp. 129-136
    • Nilges, M.1    Clore, M.2    Gronenborn, A.M.3
  • 38
    • 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 P. R., Teo C. H., 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. 372:1994;432-438.
    • (1994) Nature , vol.372 , pp. 432-438
    • Oubridge, C.1    Ito, N.2    Evans, P.R.3    Teo, C.H.4    Nagai, K.5
  • 39
    • 0028241430 scopus 로고
    • Sex determination and dosage compensation: Lessons from flies and worms
    • Parkhurst S. M., Meneely P. M. Sex determination and dosage compensation: lessons from flies and worms. Science. 264:1994;924-932.
    • (1994) Science , vol.264 , pp. 924-932
    • Parkhurst, S.M.1    Meneely, P.M.2
  • 41
    • 0027939211 scopus 로고
    • Characterization of RNA binding specificity of theDrosophilain vitro
    • Sakashita E., Sakamoto H. Characterization of RNA binding specificity of theDrosophilain vitro. Nucl. Acids Res. 22:1994;4082-4086.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 4082-4086
    • Sakashita, E.1    Sakamoto, H.2
  • 42
    • 0011092308 scopus 로고    scopus 로고
    • Protein-RNA and protein-protein interactions of theDrosophila
    • Sakashita E., Sakamoto H. Protein-RNA and protein-protein interactions of theDrosophila. J. Biochem. 120:1996.
    • (1996) J. Biochem. , vol.120
    • Sakashita, E.1    Sakamoto, H.2
  • 44
    • 0031047632 scopus 로고    scopus 로고
    • Crystal structure of the two RNA binding domains of human hnRNP A1 at 1.75 Å resolution
    • Shamoo Y., Krueger U., Rice L. M., Williams K. R., Steitz T. A. Crystal structure of the two RNA binding domains of human hnRNP A1 at 1.75 Å resolution. Nature Struct. Biol. 4:1997;215-222.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 215-222
    • Shamoo, Y.1    Krueger, U.2    Rice, L.M.3    Williams, K.R.4    Steitz, T.A.5
  • 45
    • 0029055472 scopus 로고
    • Distinct binding specificities and functions of higher eukaryotic polypyrimidine tract-binding proteins
    • Singh R., Valcárcel J., Green M. R. Distinct binding specificities and functions of higher eukaryotic polypyrimidine tract-binding proteins. Science. 268:1995;1173-1176.
    • (1995) Science , vol.268 , pp. 1173-1176
    • Singh, R.1    Valcárcel, J.2    Green, M.R.3
  • 46
    • 0027400786 scopus 로고
    • The protein Sex-lethal antagonizes the splicing factor U2AF to regulate alternative splicing of transformer pre-mRNA
    • Valcárcel J., Singh R., Zamore P. D., Green M. R. The protein Sex-lethal antagonizes the splicing factor U2AF to regulate alternative splicing of transformer pre-mRNA. Nature. 362:1993;171-175.
    • (1993) Nature , vol.362 , pp. 171-175
    • Valcárcel, J.1    Singh, R.2    Zamore, P.D.3    Green, M.R.4
  • 49
    • 0021095743 scopus 로고
    • Pseudo-structures for the 20 common amino acids for use on studies of protein conformations by measurements of intramolecular proton-proton distance constrains with nuclear magnetic resonance
    • Wüthrich K., Billetter M., Braun W. Pseudo-structures for the 20 common amino acids for use on studies of protein conformations by measurements of intramolecular proton-proton distance constrains with nuclear magnetic resonance. J. Mol. Biol. 169:1983;949-961.
    • (1983) J. Mol. Biol. , vol.169 , pp. 949-961
    • Wüthrich, K.1    Billetter, M.2    Braun, W.3
  • 50
    • 0031569797 scopus 로고    scopus 로고
    • Crystal structure of human UP1, the domain of hnRNP A1 that contains two RNA-recognition motifs
    • Xu R.-M., Jokhan L., Cheng X., Mayeda A., Krainer A. R. Crystal structure of human UP1, the domain of hnRNP A1 that contains two RNA-recognition motifs. Structure. 5:1997;559-570.
    • (1997) Structure , vol.5 , pp. 559-570
    • Xu, R.-M.1    Jokhan, L.2    Cheng, X.3    Mayeda, A.4    Krainer, A.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.