메뉴 건너뛰기




Volumn 31, Issue 6, 2008, Pages 824-834

A Solution to Limited Genomic Capacity: Using Adaptable Binding Surfaces to Assemble the Functional HIV Rev Oligomer on RNA

Author keywords

MICROBIO; PROTEINS; RNA

Indexed keywords

OLIGOMER; VIRUS RNA;

EID: 52049106911     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2008.07.016     Document Type: Article
Times cited : (96)

References (48)
  • 1
    • 0034636984 scopus 로고    scopus 로고
    • NMR structure of the HIV-1 nucleocapsid protein bound to stem-loop SL2 of the psi-RNA packaging signal. Implications for genome recognition
    • Amarasinghe G.K., De Guzman R.N., Turner R.B., Chancellor K.J., Wu Z.R., and Summers M.F. NMR structure of the HIV-1 nucleocapsid protein bound to stem-loop SL2 of the psi-RNA packaging signal. Implications for genome recognition. J. Mol. Biol. 301 (2000) 491-511
    • (2000) J. Mol. Biol. , vol.301 , pp. 491-511
    • Amarasinghe, G.K.1    De Guzman, R.N.2    Turner, R.B.3    Chancellor, K.J.4    Wu, Z.R.5    Summers, M.F.6
  • 3
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 A resolution
    • Ban N., Nissen P., Hansen J., Moore P.B., and Steitz T.A. The complete atomic structure of the large ribosomal subunit at 2.4 A resolution. Science 289 (2000) 905-920
    • (2000) Science , vol.289 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 5
    • 28344450939 scopus 로고    scopus 로고
    • Arginine-rich motifs present multiple interfaces for specific binding by RNA
    • Bayer T.S., Booth L.N., Knudsen S.M., and Ellington A.D. Arginine-rich motifs present multiple interfaces for specific binding by RNA. RNA 11 (2005) 1848-1857
    • (2005) RNA , vol.11 , pp. 1848-1857
    • Bayer, T.S.1    Booth, L.N.2    Knudsen, S.M.3    Ellington, A.D.4
  • 6
    • 0031567148 scopus 로고    scopus 로고
    • A dynamic in vivo view of the HIV-I Rev-RRE interaction
    • Charpentier B., Stutz F., and Rosbash M. A dynamic in vivo view of the HIV-I Rev-RRE interaction. J. Mol. Biol. 266 (1997) 950-962
    • (1997) J. Mol. Biol. , vol.266 , pp. 950-962
    • Charpentier, B.1    Stutz, F.2    Rosbash, M.3
  • 7
    • 0025810027 scopus 로고
    • Characterization of HIV-1 REV protein: binding stoichiometry and minimal RNA substrate
    • Cook K.S., Fisk G.J., Hauber J., Usman N., Daly T.J., and Rusche J.R. Characterization of HIV-1 REV protein: binding stoichiometry and minimal RNA substrate. Nucleic Acids Res. 19 (1991) 1577-1583
    • (1991) Nucleic Acids Res. , vol.19 , pp. 1577-1583
    • Cook, K.S.1    Fisk, G.J.2    Hauber, J.3    Usman, N.4    Daly, T.J.5    Rusche, J.R.6
  • 8
    • 0032581976 scopus 로고    scopus 로고
    • Retroviruses as model systems for the study of nuclear RNA export pathways
    • Cullen B.R. Retroviruses as model systems for the study of nuclear RNA export pathways. Virology 249 (1998) 203-210
    • (1998) Virology , vol.249 , pp. 203-210
    • Cullen, B.R.1
  • 9
    • 0042658190 scopus 로고    scopus 로고
    • Nuclear mRNA export: insights from virology
    • Cullen B.R. Nuclear mRNA export: insights from virology. Trends Biochem. Sci. 28 (2003) 419-424
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 419-424
    • Cullen, B.R.1
  • 11
    • 39549100997 scopus 로고    scopus 로고
    • Protein structure and oligomerization are important for the formation of export-competent HIV-1 Rev-RRE complexes
    • Edgcomb S.P., Aschrafi A., Kompfner E., Williamson J.R., Gerace L., and Hennig M. Protein structure and oligomerization are important for the formation of export-competent HIV-1 Rev-RRE complexes. Protein Sci. 17 (2008) 420-430
    • (2008) Protein Sci. , vol.17 , pp. 420-430
    • Edgcomb, S.P.1    Aschrafi, A.2    Kompfner, E.3    Williamson, J.R.4    Gerace, L.5    Hennig, M.6
  • 12
    • 0030924190 scopus 로고    scopus 로고
    • CRM1 is an export receptor for leucine-rich nuclear export signals
    • Fornerod M., Ohno M., Yoshida M., and Mattaj I.W. CRM1 is an export receptor for leucine-rich nuclear export signals. Cell 90 (1997) 1051-1060
    • (1997) Cell , vol.90 , pp. 1051-1060
    • Fornerod, M.1    Ohno, M.2    Yoshida, M.3    Mattaj, I.W.4
  • 13
    • 27444442727 scopus 로고    scopus 로고
    • HIV-1 Rev oligomerization is not obligatory in the presence of an extra basic domain
    • Furnes C., Arnesen T., Askjaer P., Kjems J., and Szilvay A.M. HIV-1 Rev oligomerization is not obligatory in the presence of an extra basic domain. Retrovirology 2 (2005) 39
    • (2005) Retrovirology , vol.2 , pp. 39
    • Furnes, C.1    Arnesen, T.2    Askjaer, P.3    Kjems, J.4    Szilvay, A.M.5
  • 14
    • 52049116251 scopus 로고    scopus 로고
    • Goddard, T.D., and Kneller, D.G. (2007). SPARKY 3.112, University of California, San Francisco.
    • Goddard, T.D., and Kneller, D.G. (2007). SPARKY 3.112, University of California, San Francisco.
  • 15
    • 0037071839 scopus 로고    scopus 로고
    • Structure of the SRP19 RNA complex and implications for signal recognition particle assembly
    • Hainzl T., Huang S., and Sauer-Eriksson A.E. Structure of the SRP19 RNA complex and implications for signal recognition particle assembly. Nature 417 (2002) 767-771
    • (2002) Nature , vol.417 , pp. 767-771
    • Hainzl, T.1    Huang, S.2    Sauer-Eriksson, A.E.3
  • 16
    • 0141707094 scopus 로고    scopus 로고
    • Structural basis of a phototropin light switch
    • Harper S.M., Neil L.C., and Gardner K.H. Structural basis of a phototropin light switch. Science 301 (2003) 1541-1544
    • (2003) Science , vol.301 , pp. 1541-1544
    • Harper, S.M.1    Neil, L.C.2    Gardner, K.H.3
  • 17
    • 0001926296 scopus 로고    scopus 로고
    • Virus structure
    • Fields B.N. (Ed), Lippincott-Raven, Philadelphia
    • Harrison S.C., Skehel J.J., and Wiley D.C. Virus structure. In: Fields B.N. (Ed). Virology (1996), Lippincott-Raven, Philadelphia 59-99
    • (1996) Virology , pp. 59-99
    • Harrison, S.C.1    Skehel, J.J.2    Wiley, D.C.3
  • 18
    • 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 J.T., Gait M.J., Karn J., and Singh M. 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 (1991) 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
  • 19
    • 0025149054 scopus 로고
    • Mutational analysis of the human immunodeficiency virus type 1 Rev transactivator: essential residues near the amino terminus
    • Hope T.J., McDonald D., Huang X.J., Low J., and Parslow T.G. Mutational analysis of the human immunodeficiency virus type 1 Rev transactivator: essential residues near the amino terminus. J. Virol. 64 (1990) 5360-5366
    • (1990) J. Virol. , vol.64 , pp. 5360-5366
    • Hope, T.J.1    McDonald, D.2    Huang, X.J.3    Low, J.4    Parslow, T.G.5
  • 20
    • 0026089413 scopus 로고
    • Minimal Rev-response element for Type 1 human immunodeficiency virus
    • Huang X., Hope T.J., Bond B.L., McDonald D., Grahl K., and Parslow T.G. Minimal Rev-response element for Type 1 human immunodeficiency virus. J. Virol. 65 (1991) 2131-2134
    • (1991) J. Virol. , vol.65 , pp. 2131-2134
    • Huang, X.1    Hope, T.J.2    Bond, B.L.3    McDonald, D.4    Grahl, K.5    Parslow, T.G.6
  • 21
    • 0027104999 scopus 로고
    • Recognition of the high affinity binding site in rev-response element RNA by the human immunodeficiency virus type-1 rev protein
    • Iwai S., Pritchard C., Mann D.A., Karn J., and Gait M.J. Recognition of the high affinity binding site in rev-response element RNA by the human immunodeficiency virus type-1 rev protein. Nucleic Acids Res. 20 (1992) 6465-6472
    • (1992) Nucleic Acids Res. , vol.20 , pp. 6465-6472
    • Iwai, S.1    Pritchard, C.2    Mann, D.A.3    Karn, J.4    Gait, M.J.5
  • 22
    • 0030272096 scopus 로고    scopus 로고
    • A structural model for the HIV-1 Rev-RRE complex deduced from altered-specificity rev variants isolated by a rapid genetic strategy
    • Jain C., and Belasco J.G. A structural model for the HIV-1 Rev-RRE complex deduced from altered-specificity rev variants isolated by a rapid genetic strategy. Cell 87 (1996) 115-125
    • (1996) Cell , vol.87 , pp. 115-125
    • Jain, C.1    Belasco, J.G.2
  • 23
    • 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., and Belasco J.G. 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 (2001) 603-614
    • (2001) Mol. Cell , vol.7 , pp. 603-614
    • Jain, C.1    Belasco, J.G.2
  • 24
    • 0026034946 scopus 로고
    • Structural analysis of the interaction between the human immunodeficiency virus Rev protein and the Rev response element
    • Kjems J., Brown M., Chang D.D., and Sharp P.A. Structural analysis of the interaction between the human immunodeficiency virus Rev protein and the Rev response element. Proc. Natl. Acad. Sci. USA 88 (1991) 683-687
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 683-687
    • Kjems, J.1    Brown, M.2    Chang, D.D.3    Sharp, P.A.4
  • 25
    • 0027283983 scopus 로고
    • The basic domain of Rev from human immunodeficiency virus type 1 specifically blocks the entry of U4/U6.U5 small nuclear ribonucleoprotein in spliceosome assembly
    • Kjems J., and Sharp P.A. The basic domain of Rev from human immunodeficiency virus type 1 specifically blocks the entry of U4/U6.U5 small nuclear ribonucleoprotein in spliceosome assembly. J. Virol. 67 (1993) 4769-4776
    • (1993) J. Virol. , vol.67 , pp. 4769-4776
    • Kjems, J.1    Sharp, P.A.2
  • 26
    • 23644444928 scopus 로고    scopus 로고
    • A simple motif for protein recognition in DNA secondary structures
    • Landt S.G., Ramirez A., Daugherty M.D., and Frankel A.D. A simple motif for protein recognition in DNA secondary structures. J. Mol. Biol. 351 (2005) 982-994
    • (2005) J. Mol. Biol. , vol.351 , pp. 982-994
    • Landt, S.G.1    Ramirez, A.2    Daugherty, M.D.3    Frankel, A.D.4
  • 27
    • 34249316905 scopus 로고    scopus 로고
    • RNA-binding proteins: modular design for efficient function
    • Lunde B.M., Moore C., and Varani G. RNA-binding proteins: modular design for efficient function. Nat. Rev. Mol. Cell Biol. 8 (2007) 479-490
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 479-490
    • Lunde, B.M.1    Moore, C.2    Varani, G.3
  • 28
    • 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 M.H., and Cullen B.R. HIV-1 structural gene expression requires the binding of multiple Rev monomers to the viral RRE: implications for HIV-1 latency. Cell 65 (1991) 241-248
    • (1991) Cell , vol.65 , pp. 241-248
    • Malim, M.H.1    Cullen, B.R.2
  • 29
    • 0024518918 scopus 로고
    • The HIV-1 rev trans-activator acts through a structured target sequence to activate nuclear export of unspliced viral mRNA
    • Malim M.H., Hauber J., Le S.Y., Maizel J.V., and Cullen B.R. The HIV-1 rev trans-activator acts through a structured target sequence to activate nuclear export of unspliced viral mRNA. Nature 338 (1989) 254-257
    • (1989) Nature , vol.338 , pp. 254-257
    • Malim, M.H.1    Hauber, J.2    Le, S.Y.3    Maizel, J.V.4    Cullen, B.R.5
  • 30
    • 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 D.A., Mikaelian I., Zemmel R.W., Green S.M., Lowe A.D., Kimura T., Singh M., Butler P.J., Gait M.J., and Karn J. 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 (1994) 193-207
    • (1994) J. Mol. Biol. , vol.241 , pp. 193-207
    • Mann, D.A.1    Mikaelian, I.2    Zemmel, R.W.3    Green, S.M.4    Lowe, A.D.5    Kimura, T.6    Singh, M.7    Butler, P.J.8    Gait, M.J.9    Karn, J.10
  • 31
    • 0037472782 scopus 로고    scopus 로고
    • Modulation of DNA-binding domains for sequence-specific DNA recognition
    • Marmorstein R., and Fitzgerald M.X. Modulation of DNA-binding domains for sequence-specific DNA recognition. Gene 304 (2003) 1-12
    • (2003) Gene , vol.304 , pp. 1-12
    • Marmorstein, R.1    Fitzgerald, M.X.2
  • 32
    • 0035120436 scopus 로고    scopus 로고
    • Exchange of the basic domain of human immunodeficiency virus type 1 Rev for a polyarginine stretch expands the RNA binding specificity, and a minimal arginine cluster is required for optimal RRE RNA binding affinity, nuclear accumulation, and trans-activation
    • Nam Y.S., Petrovic A., Jeong K.S., and Venkatesan S. Exchange of the basic domain of human immunodeficiency virus type 1 Rev for a polyarginine stretch expands the RNA binding specificity, and a minimal arginine cluster is required for optimal RRE RNA binding affinity, nuclear accumulation, and trans-activation. J. Virol. 75 (2001) 2957-2971
    • (2001) J. Virol. , vol.75 , pp. 2957-2971
    • Nam, Y.S.1    Petrovic, A.2    Jeong, K.S.3    Venkatesan, S.4
  • 33
    • 0041372953 scopus 로고    scopus 로고
    • Multiple RRMs contribute to RNA binding specificity and affinity for polypyrimidine tract binding protein
    • Perez I., McAfee J.G., and Patton J.G. Multiple RRMs contribute to RNA binding specificity and affinity for polypyrimidine tract binding protein. Biochemistry 36 (1997) 11881-11890
    • (1997) Biochemistry , vol.36 , pp. 11881-11890
    • Perez, I.1    McAfee, J.G.2    Patton, J.G.3
  • 35
    • 0028907506 scopus 로고
    • Multiple RNA binding domains (RBDs) just don't add up
    • Shamoo Y., Abdul-Manan N., and Williams K.R. Multiple RNA binding domains (RBDs) just don't add up. Nucleic Acids Res. 23 (1995) 725-728
    • (1995) Nucleic Acids Res. , vol.23 , pp. 725-728
    • Shamoo, Y.1    Abdul-Manan, N.2    Williams, K.R.3
  • 36
    • 8644268780 scopus 로고    scopus 로고
    • A pathway of sequential arginine-serine-rich domain-splicing signal interactions during mammalian spliceosome assembly
    • Shen H., and Green M.R. A pathway of sequential arginine-serine-rich domain-splicing signal interactions during mammalian spliceosome assembly. Mol. Cell 16 (2004) 363-373
    • (2004) Mol. Cell , vol.16 , pp. 363-373
    • Shen, H.1    Green, M.R.2
  • 38
    • 0030738086 scopus 로고    scopus 로고
    • The effect of viral regulatory protein expression on gene delivery by human immunodeficiency virus type 1 vectors produced in stable packaging cell lines
    • Srinivasakumar N., Chazal N., Helga-Maria C., Prasad S., Hammarskjold M.L., and Rekosh D. The effect of viral regulatory protein expression on gene delivery by human immunodeficiency virus type 1 vectors produced in stable packaging cell lines. J. Virol. 71 (1997) 5841-5848
    • (1997) J. Virol. , vol.71 , pp. 5841-5848
    • Srinivasakumar, N.1    Chazal, N.2    Helga-Maria, C.3    Prasad, S.4    Hammarskjold, M.L.5    Rekosh, D.6
  • 39
    • 0032901069 scopus 로고    scopus 로고
    • Polyvalent Rev decoys act as artificial Rev-responsive elements
    • Symensma T.L., Baskerville S., Yan A., and Ellington A.D. Polyvalent Rev decoys act as artificial Rev-responsive elements. J. Virol. 73 (1999) 4341-4349
    • (1999) J. Virol. , vol.73 , pp. 4341-4349
    • Symensma, T.L.1    Baskerville, S.2    Yan, A.3    Ellington, A.D.4
  • 41
    • 0028596537 scopus 로고
    • Costabilization of peptide and RNA structure in an HIV Rev peptide-RRE complex
    • Tan R., and Frankel A.D. Costabilization of peptide and RNA structure in an HIV Rev peptide-RRE complex. Biochemistry 33 (1994) 14579-14585
    • (1994) Biochemistry , vol.33 , pp. 14579-14585
    • Tan, R.1    Frankel, A.D.2
  • 42
    • 0026601935 scopus 로고
    • Identification of a high-affinity RNA-binding site for the human immunodeficiency virus type 1 Rev protein
    • Tiley L.S., Malim M.H., Tewary H.K., Stockley P.G., and Cullen B.R. Identification of a high-affinity RNA-binding site for the human immunodeficiency virus type 1 Rev protein. Proc. Natl. Acad. Sci. USA 89 (1992) 758-762
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 758-762
    • Tiley, L.S.1    Malim, M.H.2    Tewary, H.K.3    Stockley, P.G.4    Cullen, B.R.5
  • 43
    • 0036129107 scopus 로고    scopus 로고
    • Probability-based protein secondary structure identification using combined NMR chemical-shift data
    • Wang Y., and Jardetzky O. Probability-based protein secondary structure identification using combined NMR chemical-shift data. Protein Sci. 11 (2002) 852-861
    • (2002) Protein Sci. , vol.11 , pp. 852-861
    • Wang, Y.1    Jardetzky, O.2
  • 44
    • 0029130168 scopus 로고
    • Identification of a signal for rapid export of proteins from the nucleus
    • Wen W., Meinkoth J.L., Tsien R.Y., and Taylor S.S. Identification of a signal for rapid export of proteins from the nucleus. Cell 82 (1995) 463-473
    • (1995) Cell , vol.82 , pp. 463-473
    • Wen, W.1    Meinkoth, J.L.2    Tsien, R.Y.3    Taylor, S.S.4
  • 45
    • 0029847929 scopus 로고    scopus 로고
    • Anti-peptide aptamers recognize amino acid sequence and bind a protein epitope
    • Xu W., and Ellington A.D. Anti-peptide aptamers recognize amino acid sequence and bind a protein epitope. Proc. Natl. Acad. Sci. USA 93 (1996) 7475-7480
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7475-7480
    • Xu, W.1    Ellington, A.D.2
  • 47
    • 3042798454 scopus 로고    scopus 로고
    • Yeast telomerase RNA: a flexible scaffold for protein subunits
    • Zappulla D.C., and Cech T.R. Yeast telomerase RNA: a flexible scaffold for protein subunits. Proc. Natl. Acad. Sci. USA 101 (2004) 10024-10029
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 10024-10029
    • Zappulla, D.C.1    Cech, T.R.2
  • 48
    • 0029933537 scopus 로고    scopus 로고
    • Flexible regions of RNA structure facilitate co-operative Rev assembly on the Rev-response element
    • Zemmel R.W., Kelley A.C., Karn J., and Butler P.J. Flexible regions of RNA structure facilitate co-operative Rev assembly on the Rev-response element. J. Mol. Biol. 258 (1996) 763-777
    • (1996) J. Mol. Biol. , vol.258 , pp. 763-777
    • Zemmel, R.W.1    Kelley, A.C.2    Karn, J.3    Butler, P.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.