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Volumn 107, Issue 28, 2010, Pages 12481-12486

HIV Rev response element (RRE) directs assembly of the Rev homooligomer into discrete asymmetric complexes

Author keywords

Nuclear export; Ribonucleoprotein assembly; RNA protein recognition

Indexed keywords

MESSENGER RNA; OLIGOMER; REV PROTEIN; REV RESPONSE ELEMENT; RIBONUCLEOPROTEIN; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG; VIRUS RNA;

EID: 77955446835     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1007022107     Document Type: Article
Times cited : (65)

References (37)
  • 1
    • 0042658190 scopus 로고    scopus 로고
    • Nuclear mRNA export: Insights from virology
    • Cullen BR (2003) Nuclear mRNA export: Insights from virology. Trends Biochem Sci 28:419-424.
    • (2003) Trends Biochem Sci , vol.28 , pp. 419-424
    • Cullen, B.R.1
  • 3
    • 0025818452 scopus 로고
    • HIV-1 structural gene expression requires the binding of multiple Rev monomers to the viral RRE: Implications for HIV-1 latency
    • Malim MH, Cullen BR (1991) HIV-1 structural gene expression requires the binding of multiple Rev monomers to the viral RRE: Implications for HIV-1 latency. Cell 65:241-248.
    • (1991) Cell , vol.65 , pp. 241-248
    • Malim, M.H.1    Cullen, B.R.2
  • 4
    • 0025190644 scopus 로고
    • HIV-1 structural gene expression requires binding of the rev trans-activator to its RNA target sequence
    • DOI 10.1016/0092-8674(90)90670-A
    • Malim MH, et al. (1990) HIV-1 structural gene expression requires binding of the Rev trans-activator to its RNA target sequence. Cell 60:675-683. (Pubitemid 20083823)
    • (1990) Cell , vol.60 , Issue.4 , pp. 675-683
    • Malim, M.H.1    Tiley, L.S.2    McCarn, D.F.3    Rusche, J.R.4    Hauber, J.5    Cullen, B.R.6
  • 5
    • 0026089413 scopus 로고
    • Minimal Rev-response element for Type 1 human immunodeficiency virus
    • Huang X, et al. (1991) Minimal Rev-response element for Type 1 human immunodeficiency virus. J Virol 65:2131-2134.
    • (1991) J Virol , vol.65 , pp. 2131-2134
    • Huang, X.1
  • 6
    • 0028108364 scopus 로고
    • A molecular rheostat: Co-operative rev binding to stem I of the Rev-response element modulates human immunodeficiency virus type-1 late gene expression
    • Mann DA, et al. (1994) A molecular rheostat: Co-operative rev binding to stem I of the Rev-response element modulates human immunodeficiency virus type-1 late gene expression. J Mol Biol 241:193-207.
    • (1994) J Mol Biol , vol.241 , pp. 193-207
    • Mann, D.A.1
  • 7
    • 0029784592 scopus 로고    scopus 로고
    • Alpha helix-RNA major groove recognition in an HIV-1 Rev peptide-RRE RNA complex
    • Battiste JL, et al. (1996) Alpha helix-RNA major groove recognition in an HIV-1 Rev peptide-RRE RNA complex. Science 273:1547-1551.
    • (1996) Science , vol.273 , pp. 1547-1551
    • Battiste, J.L.1
  • 8
    • 0027251792 scopus 로고
    • RNA recognition by an isolated alpha helix
    • DOI 10.1016/0092-8674(93)90280-4
    • Tan R, Chen L, Buettner JA, Hudson D, Frankel AD (1993) RNA recognition by an isolated alpha helix. Cell 73:1031-1040. (Pubitemid 23165617)
    • (1993) Cell , vol.73 , Issue.5 , pp. 1031-1040
    • Tan, R.1    Chen, L.2    Buettner, J.A.3    Hudson, D.4    Frankel, A.D.5
  • 9
    • 52049106911 scopus 로고    scopus 로고
    • A solution to limited genomic capacity: Using adaptable binding surfaces to assemble the functional HIV Rev oligomer on RNA
    • Daugherty MD, D'Orso I, Frankel AD (2008) A solution to limited genomic capacity: Using adaptable binding surfaces to assemble the functional HIV Rev oligomer on RNA. Mol Cell 31:824-834.
    • (2008) Mol Cell , vol.31 , pp. 824-834
    • Daugherty, M.D.1    D'Orso, I.2    Frankel, A.D.3
  • 11
    • 77950539375 scopus 로고    scopus 로고
    • Implications of the HIV-1 Rev dimer structure at 3.2 A resolution for multimeric binding to the Rev response element
    • Dimattia MA, et al. (2010) Implications of the HIV-1 Rev dimer structure at 3.2 A resolution for multimeric binding to the Rev response element. Proc Natl Acad Sci USA 107:5810-5814.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 5810-5814
    • Dimattia, M.A.1
  • 12
    • 0035265946 scopus 로고    scopus 로고
    • Structural model for the cooperative assembly of HIV-1 Rev multimers on the RRE as deduced from analysis of assembly-defective mutants
    • Jain C, Belasco JG (2001) Structural model for the cooperative assembly of HIV-1 Rev multimers on the RRE as deduced from analysis of assembly-defective mutants. Mol Cell 7:603-614.
    • (2001) Mol Cell , vol.7 , pp. 603-614
    • Jain, C.1    Belasco, J.G.2
  • 13
    • 0025882673 scopus 로고
    • Human immunodeficiency virus type 1 regulator of virion expression, rev, forms nucleoprotein filaments after binding to a purine-rich "bubble" located within the rev-responsive region of viral mRNAs
    • Heaphy S, Finch JT, Gait MJ, Karn J, Singh M (1991) Human immunodeficiency virus type 1 regulator of virion expression, rev, forms nucleoprotein filaments after binding to a purine-rich "bubble" located within the rev-responsive region of viral mRNAs. Proc Natl Acad Sci USA 88:7366-7370.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 7366-7370
    • Heaphy, S.1    Finch, J.T.2    Gait, M.J.3    Karn, J.4    Singh, M.5
  • 14
    • 0025871993 scopus 로고
    • HIV-1 Rev expressed in recombinant Escherichia coli: Purification, polymerization, and conformational properties
    • Wingfield PT, et al. (1991) HIV-1 Rev expressed in recombinant Escherichia coli: Purification, polymerization, and conformational properties. Biochemistry 30:7527-7534.
    • (1991) Biochemistry , vol.30 , pp. 7527-7534
    • Wingfield, P.T.1
  • 15
    • 0027437477 scopus 로고
    • Solution oligomerization of the rev protein of HIV-1: Implications for function
    • Cole JL, Gehman JD, Shafer JA, Kuo LC (1993) Solution oligomerization of the rev protein of HIV-1: Implications for function. Biochemistry 32:11769-11775.
    • (1993) Biochemistry , vol.32 , pp. 11769-11775
    • Cole, J.L.1    Gehman, J.D.2    Shafer, J.A.3    Kuo, L.C.4
  • 16
    • 33947359134 scopus 로고    scopus 로고
    • Constraints on protein structure in HIV-1 Rev and Rev-RNA supramolecular assemblies from two-dimensional solid state nuclear magnetic resonance
    • Havlin RH, Blanco FJ, Tycko R (2007) Constraints on protein structure in HIV-1 Rev and Rev-RNA supramolecular assemblies from two-dimensional solid state nuclear magnetic resonance. Biochemistry 46:3586-3593.
    • (2007) Biochemistry , vol.46 , pp. 3586-3593
    • Havlin, R.H.1    Blanco, F.J.2    Tycko, R.3
  • 17
    • 77649176543 scopus 로고    scopus 로고
    • Overcoming the solubility limit with solubility-enhancement tags: Successful applications in biomolecular NMR studies
    • Zhou P, Wagner G (2009) Overcoming the solubility limit with solubility-enhancement tags: Successful applications in biomolecular NMR studies. J Biomol NMR 46:23-31.
    • (2009) J Biomol NMR , vol.46 , pp. 23-31
    • Zhou, P.1    Wagner, G.2
  • 18
    • 0031927429 scopus 로고    scopus 로고
    • Three-dimensional structure of HIV-1 Rev protein filaments
    • Watts NR, et al. (1998) Three-dimensional structure of HIV-1 Rev protein filaments. J Struct Biol 121:41-52.
    • (1998) J Struct Biol , vol.121 , pp. 41-52
    • Watts, N.R.1
  • 19
    • 0035798396 scopus 로고    scopus 로고
    • Solid-state NMR data support a helix-loop-helix structural model for the N-terminal half of HIV-1 Rev in fibrillar form
    • DOI 10.1006/jmbi.2001.5067
    • Blanco FJ, Hess S, Pannell LK, Rizzo NW, Tycko R (2001) Solid-state NMR data support a helix-loop-helix structural model for the N-terminal half of HIV-1 Rev in fibrillar form. J Mol Biol 313:845-859. (Pubitemid 33063431)
    • (2001) Journal of Molecular Biology , vol.313 , Issue.4 , pp. 845-859
    • Blanco, F.J.1    Hess, S.2    Pannell, L.K.3    Rizzo, N.W.4    Tycko, R.5
  • 20
    • 0345169163 scopus 로고    scopus 로고
    • Small-angle scattering: A view on the properties, structures and structural changes of biological macromolecules in solution
    • Koch MH, Vachette P, Svergun DI (2003) Small-angle scattering: a view on the properties, structures and structural changes of biological macromolecules in solution. Q Rev Biophys 36:147-227.
    • (2003) Q Rev Biophys , vol.36 , pp. 147-227
    • Koch, M.H.1    Vachette, P.2    Svergun, D.I.3
  • 21
    • 0028295562 scopus 로고
    • Helix-loop-helix motif in HIV-1 Rev
    • Auer M, et al. (1994) Helix-loop-helix motif in HIV-1 Rev. Biochemistry 33:2988-2996.
    • (1994) Biochemistry , vol.33 , pp. 2988-2996
    • Auer, M.1
  • 22
    • 0036129107 scopus 로고    scopus 로고
    • Probability-based protein secondary structure identification using combined NMR chemical-shift data
    • DOI 10.1110/ps.3180102
    • Wang Y, Jardetzky O (2002) Probability-based protein secondary structure identification using combined NMR chemical-shift data. Protein Sci 11:852-861. (Pubitemid 34241293)
    • (2002) Protein Science , vol.11 , Issue.4 , pp. 852-861
    • Wang, Y.1    Jardetzky, O.2
  • 23
    • 0024449503 scopus 로고
    • Backbone dynamics of proteins as studied by 15 N inverse detected heteronuclear NMR spectroscopy: Application to staphylococcal nuclease
    • Kay LE, Torchia DA, Bax A (1989) Backbone dynamics of proteins as studied by 15 N inverse detected heteronuclear NMR spectroscopy: Application to staphylococcal nuclease. Biochemistry 28:8972-8979.
    • (1989) Biochemistry , vol.28 , pp. 8972-8979
    • Kay, L.E.1    Torchia, D.A.2    Bax, A.3
  • 24
    • 33746558802 scopus 로고    scopus 로고
    • Crystal structure of the rabies virus nucleoprotein-RNA complex
    • Albertini AA, et al. (2006) Crystal structure of the rabies virus nucleoprotein-RNA complex. Science 313:360-363.
    • (2006) Science , vol.313 , pp. 360-363
    • Albertini, A.A.1
  • 25
    • 63649099704 scopus 로고    scopus 로고
    • Crystal structure of human spliceosomal U1 snRNP at 5.5 A resolution
    • Pomeranz Krummel DA, Oubridge C, Leung AK, Li J, Nagai K (2009) Crystal structure of human spliceosomal U1 snRNP at 5.5 A resolution. Nature 458:475-480.
    • (2009) Nature , vol.458 , pp. 475-480
    • Pomeranz Krummel, D.A.1    Oubridge, C.2    Leung, A.K.3    Li, J.4    Nagai, K.5
  • 26
    • 70849108252 scopus 로고    scopus 로고
    • Crystal structure of a nucleocapsid-like nucleoprotein-RNA complex of respiratory syncytial virus
    • Tawar RG, et al. (2009) Crystal structure of a nucleocapsid-like nucleoprotein-RNA complex of respiratory syncytial virus. Science 326:1279-1283.
    • (2009) Science , vol.326 , pp. 1279-1283
    • Tawar, R.G.1
  • 27
    • 69449095153 scopus 로고    scopus 로고
    • Promiscuous substrate recognition in folding and assembly activities of the trigger factor chaperone
    • Martinez-Hackert E, Hendrickson WA (2009) Promiscuous substrate recognition in folding and assembly activities of the trigger factor chaperone. Cell 138:923-934.
    • (2009) Cell , vol.138 , pp. 923-934
    • Martinez-Hackert, E.1    Hendrickson, W.A.2
  • 28
    • 77649336166 scopus 로고    scopus 로고
    • Generation and characterization of a chimeric rabbit/human Fab for co-crystallization of HIV-1 Rev
    • Stahl SJ, et al. (2010) Generation and characterization of a chimeric rabbit/human Fab for co-crystallization of HIV-1 Rev. J Mol Biol 397:697-708.
    • (2010) J Mol Biol , vol.397 , pp. 697-708
    • Stahl, S.J.1
  • 29
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 A resolution
    • DOI 10.1126/science.289.5481.905
    • Ban N, Nissen P, Hansen J, Moore PB, Steitz TA (2000) The complete atomic structure of the large ribosomal subunit at 2.4 A resolution. Science 289:905-920. (Pubitemid 30659939)
    • (2000) Science , vol.289 , Issue.5481 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 31
    • 0035341325 scopus 로고    scopus 로고
    • RNA binding in an Sm core domain: X-ray structure and functional analysis of an archaeal Sm protein complex
    • Toro I, et al. (2001) RNA binding in an Sm core domain: X-ray structure and functional analysis of an archaeal Sm protein complex. EMBO J 20:2293-2303.
    • (2001) EMBO J , vol.20 , pp. 2293-2303
    • Toro, I.1
  • 32
    • 0036645689 scopus 로고    scopus 로고
    • Structures of the pleiotropic translational regulator Hfq and an Hfq-RNA complex: A bacterial Sm-like protein
    • DOI 10.1093/emboj/cdf322
    • Schumacher MA, Pearson RF, Moller T, Valentin-Hansen P, Brennan RG (2002) Structures of the pleiotropic translational regulator Hfq and an Hfq-RNA complex: A bacterial Sm-like protein. EMBO J 21:3546-3556. (Pubitemid 34760584)
    • (2002) EMBO Journal , vol.21 , Issue.13 , pp. 3546-3556
    • Schumacher, M.A.1    Pearson, R.F.2    Moller, T.3    Valentin-Hansen, P.4    Brennan, R.G.5
  • 33
    • 47649126376 scopus 로고    scopus 로고
    • Cooperativity in macromolecular assembly
    • Williamson JR (2008) Cooperativity in macromolecular assembly. Nat Chem Biol 4:458-465.
    • (2008) Nat Chem Biol , vol.4 , pp. 458-465
    • Williamson, J.R.1
  • 34
    • 69249083558 scopus 로고    scopus 로고
    • Grp94, the endoplasmic reticulum Hsp90, has a similar solution conformation to cytosolic Hsp90 in the absence of nucleotide
    • Krukenberg KA, Bottcher UM, Southworth DR, Agard DA (2009) Grp94, the endoplasmic reticulum Hsp90, has a similar solution conformation to cytosolic Hsp90 in the absence of nucleotide. Protein Sci 18:1815-1827.
    • (2009) Protein Sci , vol.18 , pp. 1815-1827
    • Krukenberg, K.A.1    Bottcher, U.M.2    Southworth, D.R.3    Agard, D.A.4
  • 35
    • 2342662152 scopus 로고    scopus 로고
    • Negative staining and image classification - Powerful tools in modern electron microscopy
    • Ohi M, Li Y, Cheng Y, Walz T (2004) Negative staining and image classification - Powerful tools in modern electron microscopy. Biol Proced Online 6:23-34.
    • (2004) Biol Proced Online , vol.6 , pp. 23-34
    • Ohi, M.1    Li, Y.2    Cheng, Y.3    Walz, T.4
  • 36
    • 0032815040 scopus 로고    scopus 로고
    • Ximdisp - A visualization tool to aid structure determination from electron microscope images
    • Smith JM (1999) Ximdisp - A visualization tool to aid structure determination from electron microscope images. J Struct Biol 125:223-228.
    • (1999) J Struct Biol , vol.125 , pp. 223-228
    • Smith, J.M.1
  • 37
    • 58049204808 scopus 로고    scopus 로고
    • SPIDER image processing for single-particle reconstruction of biological macromolecules from electron micrographs
    • Shaikh TR, et al. (2008) SPIDER image processing for single-particle reconstruction of biological macromolecules from electron micrographs. Nat Protoc 3:1941-1974.
    • (2008) Nat Protoc , vol.3 , pp. 1941-1974
    • Shaikh, T.R.1


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