메뉴 건너뛰기




Volumn 45, Issue 12, 2006, Pages 3943-3951

Molecular recognition of an RNA trafficking element by heterogeneous nuclear ribonucleoprotein A2

Author keywords

[No Author keywords available]

Indexed keywords

NUCLEIC ACIDS; PROTEINS; RNA; SPECTROSCOPIC ANALYSIS;

EID: 33645455276     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi052440e     Document Type: Article
Times cited : (13)

References (51)
  • 1
    • 0033134777 scopus 로고    scopus 로고
    • Crystal structure of the two-RRM domain of hnRNP A1 (UP1) complexed with single-stranded telomeric DNA
    • Ding, J., Hayashi, M. K., Zhang, Y., Manche, L., Krainer, A. R., and Xu, R. M. (1999) Crystal structure of the two-RRM domain of hnRNP A1 (UP1) complexed with single-stranded telomeric DNA, Genes Dev. 13, 1102-1115.
    • (1999) Genes Dev. , vol.13 , pp. 1102-1115
    • Ding, J.1    Hayashi, M.K.2    Zhang, Y.3    Manche, L.4    Krainer, A.R.5    Xu, R.M.6
  • 2
    • 0034623948 scopus 로고    scopus 로고
    • Binding of an RNA trafficking response element to heterogeneous nuclear ribonucleoproteins A1 and A2
    • Shan, J., Moran-Jones, K., Munro, T. P., Kidd, G. J., Winzor, D. J., Hoek, K. S., and Smith, R. (2000) Binding of an RNA trafficking response element to heterogeneous nuclear ribonucleoproteins A1 and A2, J. Biol. Chem. 275, 38286-38295.
    • (2000) J. Biol. Chem. , vol.275 , pp. 38286-38295
    • Shan, J.1    Moran-Jones, K.2    Munro, T.P.3    Kidd, G.J.4    Winzor, D.J.5    Hoek, K.S.6    Smith, R.7
  • 3
    • 0032516935 scopus 로고    scopus 로고
    • The heterogeneous nuclear ribonucleoprotein C protein tetramer binds U1, U2, and U6 snRNAs through its high affinity RNA binding domain (the bZIP-like motif)
    • Shahied-Milam, L., Soltaninassab, S. R., Iyer, G. V., and LeStourgeon, W. M. (1998) The heterogeneous nuclear ribonucleoprotein C protein tetramer binds U1, U2, and U6 snRNAs through its high affinity RNA binding domain (the bZIP-like motif), J. Biol. Chem. 273, 21359-21367.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21359-21367
    • Shahied-Milam, L.1    Soltaninassab, S.R.2    Iyer, G.V.3    LeStourgeon, W.M.4
  • 7
    • 0028061367 scopus 로고
    • Function of conserved domains of hnRNP A1 and other hnRNP A/B proteins
    • Mayeda, A., Munroe, S. H., Caceres, J. F., and Krainer, A. R. (1994) Function of conserved domains of hnRNP A1 and other hnRNP A/B proteins, EMBO J. 13, 5483-5495.
    • (1994) EMBO J. , vol.13 , pp. 5483-5495
    • Mayeda, A.1    Munroe, S.H.2    Caceres, J.F.3    Krainer, A.R.4
  • 8
    • 0032753210 scopus 로고    scopus 로고
    • The cis-acting RNA trafficking signal from myelin basic protein mRNA and its cognate trans-acting ligand hnRNP A2 enhance cap-dependent translation
    • Kwon, S., Barbarese, E., and Carson, J. H. (1999) The cis-acting RNA trafficking signal from myelin basic protein mRNA and its cognate trans-acting ligand hnRNP A2 enhance cap-dependent translation, J. Cell Biol. 147, 247-256.
    • (1999) J. Cell Biol. , vol.147 , pp. 247-256
    • Kwon, S.1    Barbarese, E.2    Carson, J.H.3
  • 9
    • 0033607521 scopus 로고    scopus 로고
    • Mutational analysis of a heterogeneous nuclear ribonucleoprotein A2 response element for RNA trafficking
    • Munro, T. P., Magee, R. J., Kidd, G. J., Carson, J. H., Barbarese, E., Smith, L. M., and Smith, R. (1999) Mutational analysis of a heterogeneous nuclear ribonucleoprotein A2 response element for RNA trafficking, J. Biol. Chem. 274, 34389-34395.
    • (1999) J. Biol. Chem. , vol.274 , pp. 34389-34395
    • Munro, T.P.1    Magee, R.J.2    Kidd, G.J.3    Carson, J.H.4    Barbarese, E.5    Smith, L.M.6    Smith, R.7
  • 12
    • 4444283116 scopus 로고    scopus 로고
    • Human UP1 as a model for understanding purine recognition in the family of proteins containing the RNA recognition motif (RRM)
    • Myers, J. C., and Shamoo, Y. (2004) Human UP1 as a model for understanding purine recognition in the family of proteins containing the RNA recognition motif (RRM), J. Mol. Biol. 342, 743-756.
    • (2004) J. Mol. Biol. , vol.342 , pp. 743-756
    • Myers, J.C.1    Shamoo, Y.2
  • 14
    • 0029993917 scopus 로고    scopus 로고
    • Differential expression in glioblastoma multiforme and cerebral hemangioblastoma of cytoplasmic proteins that bind two different domains within the 3′-untranslated region of the human glucose transporter 1 (GLUT1) messenger RNA
    • Tsukamoto, H., Boado, R. J., and Partridge, W. M. (1996) Differential expression in glioblastoma multiforme and cerebral hemangioblastoma of cytoplasmic proteins that bind two different domains within the 3′-untranslated region of the human glucose transporter 1 (GLUT1) messenger RNA, J. Clin. Invest. 97, 2823-2832.
    • (1996) J. Clin. Invest. , vol.97 , pp. 2823-2832
    • Tsukamoto, H.1    Boado, R.J.2    Partridge, W.M.3
  • 17
    • 0034634595 scopus 로고    scopus 로고
    • The vitamin D response element-binding protein. A novel dominant-negative regulator of vitamin D-directed transactivation
    • Chen, H., Hu, B., Allegretto, E. A., and Adams, J. S. (2000) The vitamin D response element-binding protein. A novel dominant-negative regulator of vitamin D-directed transactivation, J. Biol. Chem. 275, 35557-35564.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35557-35564
    • Chen, H.1    Hu, B.2    Allegretto, E.A.3    Adams, J.S.4
  • 18
    • 0027367040 scopus 로고
    • Transport and localization of exogenous myelin basic protein mRNA microinjected into oligodendrocytes
    • Ainger, K., Avossa, D., Morgan, F., Hill, S. J., Barry, C., Barbarese, E., and Carson, J. H. (1993) Transport and localization of exogenous myelin basic protein mRNA microinjected into oligodendrocytes, J. Cell Biol. 123, 431-441.
    • (1993) J. Cell Biol. , vol.123 , pp. 431-441
    • Ainger, K.1    Avossa, D.2    Morgan, F.3    Hill, S.J.4    Barry, C.5    Barbarese, E.6    Carson, J.H.7
  • 19
    • 0032510715 scopus 로고    scopus 로고
    • hnRNP A2 selectively binds the cytoplasmic transport sequence of myelin basic protein mRNA
    • Hoek, K. S., Kidd, G. J., Carson, J. H., and Smith, R. (1998) hnRNP A2 selectively binds the cytoplasmic transport sequence of myelin basic protein mRNA, Biochemistry 37, 7021-7029.
    • (1998) Biochemistry , vol.37 , pp. 7021-7029
    • Hoek, K.S.1    Kidd, G.J.2    Carson, J.H.3    Smith, R.4
  • 20
    • 0141640944 scopus 로고    scopus 로고
    • A molecular mechanism for mRNA trafficking in neuronal dendrites
    • Shan, J., Munro, T. P., Barbarese, E., Carson, J. H., and Smith, R. (2003) A molecular mechanism for mRNA trafficking in neuronal dendrites. J. Neurosci. 23, 8859-8866.
    • (2003) J. Neurosci. , vol.23 , pp. 8859-8866
    • Shan, J.1    Munro, T.P.2    Barbarese, E.3    Carson, J.H.4    Smith, R.5
  • 21
    • 0025221731 scopus 로고
    • Crystal structure of the RNA-binding domain of the U1 small nuclear ribonucleoprotein A
    • Nagai, K., Oubridge, C., Jessen, T. H., Li, J., and Evans, P. R. (1990) Crystal structure of the RNA-binding domain of the U1 small nuclear ribonucleoprotein A, Nature 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
  • 22
    • 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., and Steitz, T. A. (1997) Crystal structure of the two RNA binding domains of human hnRNP A1 at 1.75 Å resolution, Nat. Struct. Biol. 4, 215-222.
    • (1997) Nat. 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
  • 23
    • 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., and Wemmer, D. E. (1994) Resonance assignments and solution structure of the second RNA-binding domain of Sex-lethal determined by multidimensional heteronuclear magnetic resonance, Biochemistry 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
  • 24
    • 0034692906 scopus 로고    scopus 로고
    • Solution structure of the two N-terminal RNA-binding domains of nucleolin and NMR study of the interaction with its RNA target
    • Allain, F. H., Gilbert, D. E., Bouvet, P., and Feigon, J. (2000) Solution structure of the two N-terminal RNA-binding domains of nucleolin and NMR study of the interaction with its RNA target, J. Mol. Biol. 303, 227-241.
    • (2000) J. Mol. Biol. , vol.303 , pp. 227-241
    • Allain, F.H.1    Gilbert, D.E.2    Bouvet, P.3    Feigon, J.4
  • 26
    • 0025648184 scopus 로고
    • Studies of the strand-annealing activity of mammalian hnRNP complex protein A1
    • Kumar, A., and Wilson, S. H. (1990) Studies of the strand-annealing activity of mammalian hnRNP complex protein A1, Biochemistry 29, 10717-10722.
    • (1990) Biochemistry , vol.29 , pp. 10717-10722
    • Kumar, A.1    Wilson, S.H.2
  • 27
    • 0029896047 scopus 로고    scopus 로고
    • RNP A1 selectively interacts through its Gly-rich domain with different RNA-binding proteins
    • Cartegni, L., Maconi, M., Morandi, E., Cobianchi, F., Riva, S., and Biamonti, G. (1996) hnRNP A1 selectively interacts through its Gly-rich domain with different RNA-binding proteins, J. Mol. Biol. 259, 337-348.
    • (1996) J. Mol. Biol. , vol.259 , pp. 337-348
    • Cartegni, L.1    Maconi, M.2    Morandi, E.3    Cobianchi, F.4    Riva, S.5    Biamonti, G.6
  • 28
    • 0027987929 scopus 로고
    • Making a connection: Direct binding between keratin intermediate filaments and desmosomal proteins
    • Kouklis, P. D., Hutton, E., and Fuchs, E. (1994) Making a connection: Direct binding between keratin intermediate filaments and desmosomal proteins, J. Cell Biol. 127, 1049-1060.
    • (1994) J. Cell Biol. , vol.127 , pp. 1049-1060
    • Kouklis, P.D.1    Hutton, E.2    Fuchs, E.3
  • 29
    • 18744373599 scopus 로고    scopus 로고
    • A role for the 1A and L1 rod domain segments in head domain organization and function of intermediate filaments: Structural analysis of trichocyte keratin
    • Parry, D. A., Marekov, L. N., Steinert, P. M., and Smith, T. A. (2002) A role for the 1A and L1 rod domain segments in head domain organization and function of intermediate filaments: Structural analysis of trichocyte keratin, J. Struct. Biol. 137, 97-108.
    • (2002) J. Struct. Biol. , vol.137 , pp. 97-108
    • Parry, D.A.1    Marekov, L.N.2    Steinert, P.M.3    Smith, T.A.4
  • 31
    • 0026660237 scopus 로고
    • The glycine-rich domain of nucleolin has an unusual supersecondary structure responsible for its RNA-helix-destabilizing properties
    • Ghisolfi, L., Joseph, G., Amalric, F., and Erard, M. (1992) The glycine-rich domain of nucleolin has an unusual supersecondary structure responsible for its RNA-helix-destabilizing properties, J. Biol. Chem. 267, 2955-2959.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2955-2959
    • Ghisolfi, L.1    Joseph, G.2    Amalric, F.3    Erard, M.4
  • 32
    • 0025301439 scopus 로고
    • Protein secondary structure and circular dichroism: A practical guide
    • Johnson, W. C. J. (1990) Protein secondary structure and circular dichroism: A practical guide, Proteins 7, 205-214.
    • (1990) Proteins , vol.7 , pp. 205-214
    • Johnson, W.C.J.1
  • 33
    • 0023785593 scopus 로고
    • Secondary structure of proteins through circular dichroism spectroscopy
    • Johnson, W. C. J. (1988) Secondary structure of proteins through circular dichroism spectroscopy, Annu. Rev. Biophys. Biophys. Chem. 17, 145-166.
    • (1988) Annu. Rev. Biophys. Biophys. Chem. , vol.17 , pp. 145-166
    • Johnson, W.C.J.1
  • 36
    • 0030064692 scopus 로고    scopus 로고
    • Direct analysis of solute self-association by sedimentation equilibrium
    • Wills, P. R., Jacobsen, M. P., and Winzor, D. J. (1996) Direct analysis of solute self-association by sedimentation equilibrium, Biopolymers 38, 119-130.
    • (1996) Biopolymers , vol.38 , pp. 119-130
    • Wills, P.R.1    Jacobsen, M.P.2    Winzor, D.J.3
  • 37
    • 0025287330 scopus 로고
    • Comparative modeling methods: Application to the family of the mammalian serine proteases
    • Greer, J. (1990) Comparative modeling methods: Application to the family of the mammalian serine proteases, Proteins 7, 317-334.
    • (1990) Proteins , vol.7 , pp. 317-334
    • Greer, J.1
  • 38
    • 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., and Krainer, A. R. (1997) Crystal structure of human UP1, the domain of hnRNP A1 that contains two RNA-recognition motifs Structure 5, 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
  • 39
    • 0033609121 scopus 로고    scopus 로고
    • Absence of interdomain contacts in the crystal structure of the RNA recognition motifs of Sex-lethal
    • Crowder, S. M., Kanaar, R., Rio, D. C., and Alber, T. (1999) Absence of interdomain contacts in the crystal structure of the RNA recognition motifs of Sex-lethal, Proc. Natl. Acad. Sci. U.S.A. 96, 4892-4897.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 4892-4897
    • Crowder, S.M.1    Kanaar, R.2    Rio, D.C.3    Alber, T.4
  • 40
    • 0026610767 scopus 로고
    • Assessment of protein models with three-dimensional profiles
    • Luthy, R., Bowie, J. U., and Eisenberg, D. (1992) Assessment of protein models with three-dimensional profiles, Nature 356, 83-85.
    • (1992) Nature , vol.356 , pp. 83-85
    • Luthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 41
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) PROCHECK: A program to check the stereochemical quality of protein structures, J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 42
    • 0031552362 scopus 로고    scopus 로고
    • Development and validation of a genetic algorithm for flexible docking
    • Jones, G., Willett, P., Glen, R. C., Leach, A. R., and Taylor, R. (1997) Development and validation of a genetic algorithm for flexible docking, J. Mol. Biol. 267, 727-748.
    • (1997) J. Mol. Biol. , vol.267 , pp. 727-748
    • Jones, G.1    Willett, P.2    Glen, R.C.3    Leach, A.R.4    Taylor, R.5
  • 43
    • 0019263093 scopus 로고
    • Reverse turns in peptides and proteins
    • Smith, J. A., and Pease, L. G. (1980) Reverse turns in peptides and proteins, CRC Crit. Rev. Biochem. 8, 315-399.
    • (1980) CRC Crit. Rev. Biochem. , vol.8 , pp. 315-399
    • Smith, J.A.1    Pease, L.G.2
  • 44
    • 0028959773 scopus 로고
    • Circular dichroism
    • Woody, R. (1995) Circular dichroism, Methods Enzymol. 246, 34-71.
    • (1995) Methods Enzymol. , vol.246 , pp. 34-71
    • Woody, R.1
  • 45
    • 0036529482 scopus 로고    scopus 로고
    • Correlated alternative side chain conformations in the RNA-recognition motif of heterogeneous nuclear ribonucleoprotein A1
    • Vitali, J., Ding, J., Jiang, J., Zhang, Y., Krainer, A. R., and Xu, R. M. (2002) Correlated alternative side chain conformations in the RNA-recognition motif of heterogeneous nuclear ribonucleoprotein A1, Nucleic Acids Res. 30, 1531-1538.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 1531-1538
    • Vitali, J.1    Ding, J.2    Jiang, J.3    Zhang, Y.4    Krainer, A.R.5    Xu, R.M.6
  • 46
    • 0033560881 scopus 로고    scopus 로고
    • Structural basis for recognition of the tra mRNA precursor by the Sex-lethal protein
    • Handa, N., Nureki, O., Kurimoto, K., Kim, I., Sakamoto, H., Shimura, Y., Muto, Y., and Yokoyama, S. (1999) Structural basis for recognition of the tra mRNA precursor by the Sex-lethal protein, Nature 398, 579-585.
    • (1999) Nature , vol.398 , pp. 579-585
    • Handa, N.1    Nureki, O.2    Kurimoto, K.3    Kim, I.4    Sakamoto, H.5    Shimura, Y.6    Muto, Y.7    Yokoyama, S.8
  • 47
    • 0035153840 scopus 로고    scopus 로고
    • Structural basis for recognition of AU-rich element RNA by the HuD protein
    • Wang, X., and Tanaka Hall, T. M. (2001) Structural basis for recognition of AU-rich element RNA by the HuD protein Nat. Struct. Biol. 8, 141-145.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 141-145
    • Wang, X.1    Tanaka Hall, T.M.2
  • 48
    • 0033578927 scopus 로고    scopus 로고
    • Recognition of polyadenylate RNA by the poly(A)-binding protein
    • Deo, R. C., Bonanno, J. B., Sonenberg, N., and Burley, S. K. (1999) Recognition of polyadenylate RNA by the poly(A)-binding protein, Cell 98, 835-845.
    • (1999) Cell , vol.98 , pp. 835-845
    • Deo, R.C.1    Bonanno, J.B.2    Sonenberg, N.3    Burley, S.K.4
  • 49
    • 0034672094 scopus 로고    scopus 로고
    • Molecular basis of sequence-specific recognition of pre-ribosomal RNA by nucleolin
    • Allain, F. H., Bouvet, P., Dieckmann, T., and Feigon, J. (2000) Molecular basis of sequence-specific recognition of pre-ribosomal RNA by nucleolin, EMBO J. 19, 6870-6881.
    • (2000) EMBO J. , vol.19 , pp. 6870-6881
    • Allain, F.H.1    Bouvet, P.2    Dieckmann, T.3    Feigon, J.4
  • 50
    • 23844489788 scopus 로고    scopus 로고
    • Roles of heterogeneous nuclear ribonucleoproteins A and B in cell proliferation
    • He, Y. (2005) Roles of heterogeneous nuclear ribonucleoproteins A and B in cell proliferation, J. Cell Sci. 118, 3173-3183.
    • (2005) J. Cell Sci. , vol.118 , pp. 3173-3183
    • He, Y.1
  • 51
    • 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., and Neuhaus, D. (1996) 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, 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.