메뉴 건너뛰기




Volumn 17, Issue 11, 2010, Pages 1337-1342

Structural basis for cooperative RNA binding and export complex assembly by HIV Rev

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; EXPORTIN 1; GENOMIC RNA; REV PROTEIN; RIBONUCLEOPROTEIN; STRUCTURAL PROTEIN; VIRUS RNA;

EID: 78549248443     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.1902     Document Type: Article
Times cited : (134)

References (40)
  • 1
    • 0042658190 scopus 로고    scopus 로고
    • Nuclear mRNA export: Insights from virology
    • Cullen, B.R. Nuclear mRNA export: insights from virology. Trends Biochem. Sci. 28, 419-424 (2003).
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 419-424
    • Cullen, B.R.1
  • 3
    • 0030924190 scopus 로고    scopus 로고
    • CRM1 is an export receptor for leucine-rich nuclear export signals
    • Fornerod, M., Ohno, M., Yoshida, M. & Mattaj, I.W. CRM1 is an export receptor for leucine-rich nuclear export signals. Cell 90, 1051-1060 (1997).
    • (1997) Cell , vol.90 , pp. 1051-1060
    • Fornerod, M.1    Ohno, M.2    Yoshida, M.3    Mattaj, I.W.4
  • 4
    • 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. & 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, 241-248 (1991).
    • (1991) Cell , vol.65 , pp. 241-248
    • Malim, M.H.1    Cullen, B.R.2
  • 5
    • 0028108364 scopus 로고
    • A molecular rheostat: Co-operative rev binding to stem i of the Rev-response element modulates human immunodefciency virus type-1 late gene expression
    • Mann, D.A. et al. A molecular rheostat: Co-operative rev binding to stem I of the Rev-response element modulates human immunodefciency virus type-1 late gene expression. J. Mol. Biol. 241, 193-207 (1994).
    • (1994) J. Mol. Biol , vol.241 , pp. 193-207
    • Mann, D.A.1
  • 6
    • 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, M.D., D'Orso, I. & Frankel, A.D. 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)
    • (2008) Mol. Cell , vol.31 , pp. 824-834
    • Daugherty, M.D.1    D'Orso, I.2    Frankel, A.D.3
  • 7
    • 77955446835 scopus 로고    scopus 로고
    • HIV Rev response element (RRE) directs assembly of the Rev homooligomer into discrete asymmetric complexes
    • Daugherty, M.D., Booth, D.S., Jayaraman, B., Cheng, Y. & Frankel, A.D. HIV Rev response element (RRE) directs assembly of the Rev homooligomer into discrete asymmetric complexes. Proc. Natl. Acad. Sci. USA 107, 12481-12486 (2010)
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 12481-12486
    • Daugherty, M.D.1    Booth, D.S.2    Jayaraman, B.3    Cheng, Y.4    Frankel, A.D.5
  • 8
    • 0025810027 scopus 로고
    • Characterization of HIV-1 REV protein: Binding stoichiometry and minimal RNA substrate
    • Cook, K.S. et al. Characterization of HIV-1 REV protein: binding stoichiometry and minimal RNA substrate. Nucleic Acids Res. 19, 1577-1583 (1991).
    • (1991) Nucleic Acids Res. , vol.19 , pp. 1577-1583
    • Cook, K.S.1
  • 9
    • 0025166385 scopus 로고
    • HIV-1 regulator of virion expression (Rev) protein binds to an RNA stem-loop structure located within the Rev response element region
    • Heaphy, S. et al. HIV-1 regulator of virion expression (Rev) protein binds to an RNA stem-loop structure located within the Rev response element region. Cell 60, 685-693 (1990).
    • (1990) Cell , vol.60 , pp. 685-693
    • Heaphy, S.1
  • 10
    • 0025190644 scopus 로고
    • HIV-1 structural gene expression requires binding of the Rev trans-activator to its RNA target sequence
    • Malim, M.H. et al. HIV-1 structural gene expression requires binding of the Rev trans-activator to its RNA target sequence. Cell 60, 675-683 (1990).
    • (1990) Cell , vol.60 , pp. 675-683
    • Malim, M.H.1
  • 11
    • 0026034946 scopus 로고
    • Structural analysis of the interaction between the human immunodefciency virus Rev protein and the Rev response element
    • Kjems, J., Brown, M., Chang, D.D. & Sharp, P.A. Structural analysis of the interaction between the human immunodefciency virus Rev protein and the Rev response element. Proc. Natl. Acad. Sci. USA 88, 683-687 (1991).
    • (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
  • 12
    • 0025882673 scopus 로고
    • Human immunodefciency virus type 1 regulator of virion expression rev forms nucleoprotein flaments 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. & Singh, M. Human immunodefciency virus type 1 regulator of virion expression, rev, forms nucleoprotein flaments 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).
    • (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
    • 0029784592 scopus 로고    scopus 로고
    • Alpha helix-RNA major groove recognition in an HIV-1 Rev peptide-RRE RNA complex
    • Battiste, J.L. et al. Alpha helix-RNA major groove recognition in an HIV-1 Rev peptide-RRE RNA complex. Science 273, 1547-1551 (1996).
    • (1996) Science , vol.273 , pp. 1547-1551
    • Battiste, J.L.1
  • 15
    • 0029847929 scopus 로고    scopus 로고
    • Anti-peptide aptamers recognize amino acid sequence and bind a protein epitope
    • Xu, W. & Ellington, A.D. Anti-peptide aptamers recognize amino acid sequence and bind a protein epitope. Proc. Natl. Acad. Sci. USA 93, 7475-7480 (1996)
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7475-7480
    • Xu, W.1    Ellington, A.D.2
  • 16
    • 28344450939 scopus 로고    scopus 로고
    • Arginine-rich motifs present multiple interfaces for specifc binding by RNA
    • Bayer, T.S., Booth, L.N., Knudsen, S.M. & Ellington, A.D. Arginine-rich motifs present multiple interfaces for specifc binding by RNA. RNA 11, 1848-1857 (2005).
    • (2005) RNA , vol.11 , pp. 1848-1857
    • Bayer, T.S.1    Booth, L.N.2    Knudsen, S.M.3    Ellington, A.D.4
  • 17
    • 23644444928 scopus 로고    scopus 로고
    • A simple motif for protein recognition in DNA secondary structures
    • Landt, S.G., Ramirez, A., Daugherty, M.D. & Frankel, A.D. A simple motif for protein recognition in DNA secondary structures. J. Mol. Biol. 351, 982-994 (2005).
    • (2005) J. Mol. Biol. , vol.351 , pp. 982-994
    • Landt, S.G.1    Ramirez, A.2    Daugherty, M.D.3    Frankel, A.D.4
  • 18
    • 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. & Butler, P.J. Flexible regions of RNA structure facilitate co-operative Rev assembly on the Rev-response element. J. Mol. Biol. 258, 763-777 (1996).
    • (1996) J. Mol. Biol. , vol.258 , pp. 763-777
    • Zemmel, R.W.1    Kelley, A.C.2    Karn, J.3    Butler, P.J.4
  • 19
    • 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, 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, 603-614 (2001).
    • (2001) Mol. Cell , vol.7 , pp. 603-614
    • Jain, C.1    Belasco, J.G.2
  • 20
    • 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, M.A. et al. 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).
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 5810-5814
    • Dimattia, M.A.1
  • 21
    • 0028295562 scopus 로고
    • Helix-loop-helix motif in HIV-1 Rev
    • Auer, M. et al. Helix-loop-helix motif in HIV-1 Rev. Biochemistry 33, 2988-2996 (1994).
    • (1994) Biochemistry , vol.33 , pp. 2988-2996
    • Auer, M.1
  • 22
    • 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. et al. Protein structure and oligomerization are important for the formation of export-competent HIV-1 Rev-RRE complexes. Protein Sci. 17, 420-430 (2008).
    • (2008) Protein Sci. , vol.17 , pp. 420-430
    • Edgcomb, S.P.1
  • 23
  • 24
    • 47649126376 scopus 로고    scopus 로고
    • Cooperativity in macromolecular assembly
    • Williamson, J.R. Cooperativity in macromolecular assembly. Nat. Chem. Biol. 4, 458-465 (2008).
    • (2008) Nat. Chem. Biol , vol.4 , pp. 458-465
    • Williamson, J.R.1
  • 25
    • 0035369335 scopus 로고    scopus 로고
    • Nuclear-receptor interactions on DNA-response elements
    • Khorasanizadeh, S. & Rastinejad, F. Nuclear-receptor interactions on DNA-response elements. Trends Biochem. Sci. 26, 384-390 (2001).
    • (2001) Trends Biochem. Sci , vol.26 , pp. 384-390
    • Khorasanizadeh, S.1    Rastinejad, F.2
  • 26
    • 46049113874 scopus 로고    scopus 로고
    • Structural basis for dimerization in DNA recognition by Gal4
    • Hong, M. et al. Structural basis for dimerization in DNA recognition by Gal4. Structure 16, 1019-1026 (2008).
    • (2008) Structure , vol.16 , pp. 1019-1026
    • Hong, M.1
  • 27
    • 0032485391 scopus 로고    scopus 로고
    • Structure of the DNA-binding domains from NFAT, Fos and Jun bound specifcally to DNA
    • Chen, L., Glover, J.N., Hogan, P.G., Rao, A. & Harrison, S.C. Structure of the DNA-binding domains from NFAT, Fos and Jun bound specifcally to DNA. Nature 392, 42-48 (1998)
    • (1998) Nature , vol.392 , pp. 42-48
    • Chen, L.1    Glover, J.N.2    Hogan, P.G.3    Rao, A.4    Harrison, S.C.5
  • 28
    • 0019332167 scopus 로고
    • How different amino acid sequences determine similar protein structures: The structure and evolutionary dynamics of the globins
    • Lesk, A.M. & Chothia, C. How different amino acid sequences determine similar protein structures: the structure and evolutionary dynamics of the globins. J. Mol. Biol. 136, 225-270 (1980).
    • (1980) J. Mol. Biol , vol.136 , pp. 225-270
    • Lesk, A.M.1    Chothia, C.2
  • 29
    • 36448991500 scopus 로고    scopus 로고
    • Clustal W and Clustal X version 2.0
    • Larkin, M.A. et al. Clustal W and Clustal X version 2.0. Bioinformatics 23, 2947-2948 (2007).
    • (2007) Bioinformatics , vol.23 , pp. 2947-2948
    • Larkin, M.A.1
  • 30
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specifc scoring matrices
    • Jones, D.T. Protein secondary structure prediction based on position-specifc scoring matrices. J. Mol. Biol. 292, 195-202 (1999).
    • (1999) J. Mol. Biol , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 31
    • 66249108600 scopus 로고    scopus 로고
    • Crystal structure of the nuclear export receptor CRM1 in complex with Snurportin1 and RanGTP
    • Monecke, T. et al. Crystal structure of the nuclear export receptor CRM1 in complex with Snurportin1 and RanGTP. Science 324, 1087-1091 (2009).
    • (2009) Science , vol.324 , pp. 1087-1091
    • Monecke, T.1
  • 32
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 34
    • 14244272868 scopus 로고    scopus 로고
    • PHENIX: Building new software for automated crystallographic structure determination
    • Adams, P.D. et al. PHENIX: building new software for automated crystallographic structure determination. Acta Crystallogr. D Biol. Crystallogr. 58, 1948-1954 (2002).
    • (2002) Acta Crystallogr. D Biol. Crystallogr. , vol.58 , pp. 1948-1954
    • Adams, P.D.1
  • 37
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A.J. et al. Phaser crystallographic software. J. Appl. Cryst. 40, 658-674 (2007).
    • (2007) J. Appl. Cryst. , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 38
    • 34547592557 scopus 로고    scopus 로고
    • MolProbity: All-atom contacts and structure validation for proteins and nucleic acids
    • Davis, I.W. et al. MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res. 35 (Web Server issue), W375-W383 (2007).
    • (2007) Nucleic Acids Res. , vol.35 , Issue.WEB SERVER ISSUE
    • Davis, I.W.1
  • 39
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4
    • Collaborative Computational Project Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.