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Volumn 485, Issue , 2009, Pages 271-293

Reverse two-hybrid screening to analyze protein-protein interaction of HIV-1 viral and cellular proteins

Author keywords

Interaction defective mutants; lacZ; Protein Protein interactions; Reverse two hybrid system

Indexed keywords

PROTEIN; VIRUS PROTEIN;

EID: 60349127868     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-59745-170-3_19     Document Type: Article
Times cited : (13)

References (45)
  • 1
    • 2342648913 scopus 로고    scopus 로고
    • Interaction between human immunodeficiency virus type 1 reverse transcriptase and integrase proteins
    • Hehl, E. A., Joshi, P., Kalpana, G. V., et al. (2004) Interaction between human immunodeficiency virus type 1 reverse transcriptase and integrase proteins. J Virol 78, 5056-67.
    • (2004) J Virol , vol.78 , pp. 5056-5067
    • Hehl, E.A.1    Joshi, P.2    Kalpana, G.V.3
  • 2
    • 0033019033 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 integrase protein promotes reverse transcription through specific interactions with the nucleoprotein reverse transcription complex
    • Wu, X., Liu, H., Xiao, H., et al. (1999) Human immunodeficiency virus type 1 integrase protein promotes reverse transcription through specific interactions with the nucleoprotein reverse transcription complex. J Virol 73, 2126-35.
    • (1999) J Virol , vol.73 , pp. 2126-2135
    • Wu, X.1    Liu, H.2    Xiao, H.3
  • 3
    • 2342541832 scopus 로고    scopus 로고
    • Requirement for integrase during reverse transcription of human immunodeficiency virus type 1 and the effect of cysteine mutations of integrase on its interactions with reverse transcriptase
    • Zhu, K., Dobard, C., Chow, S. A. (2004) Requirement for integrase during reverse transcription of human immunodeficiency virus type 1 and the effect of cysteine mutations of integrase on its interactions with reverse transcriptase. J Virol 78, 5045-55.
    • (2004) J Virol , vol.78 , pp. 5045-5055
    • Zhu, K.1    Dobard, C.2    Chow, S.A.3
  • 4
    • 0346036088 scopus 로고    scopus 로고
    • HIV-1 integrase forms stable tetramers and associates with LEDGF/p75 protein in human cells
    • Cherepanov, P., Maertens, G., Proost, P., et al. (2003) HIV-1 integrase forms stable tetramers and associates with LEDGF/p75 protein in human cells. J Biol Chem 278, 372-81.
    • (2003) J Biol Chem , vol.278 , pp. 372-381
    • Cherepanov, P.1    Maertens, G.2    Proost, P.3
  • 5
    • 0028566214 scopus 로고
    • Binding and stimulation of HIV-1 integrase by a human homolog of yeast transcription factor SNF5
    • Kalpana, G. V., Marmon, S., Wang, W., et al. (1994) Binding and stimulation of HIV-1 integrase by a human homolog of yeast transcription factor SNF5. Science 266, 2002-6.
    • (1994) Science , vol.266 , pp. 2002-2006
    • Kalpana, G.V.1    Marmon, S.2    Wang, W.3
  • 6
    • 0035524975 scopus 로고    scopus 로고
    • Intracellular trafficking of retroviral genomes during the early phase of infection: Viral exploitation of cellular pathways
    • Goff, S. P. (2001) Intracellular trafficking of retroviral genomes during the early phase of infection: viral exploitation of cellular pathways. J Gene Med 3, 517-28.
    • (2001) J Gene Med , vol.3 , pp. 517-528
    • Goff, S.P.1
  • 7
    • 0027207885 scopus 로고
    • Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B
    • Luban, J., Bossolt, K. L., Franke, E. K., et al. (1993) Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B. Cell 73, 1067-78.
    • (1993) Cell , vol.73 , pp. 1067-1078
    • Luban, J.1    Bossolt, K.L.2    Franke, E.K.3
  • 8
    • 0033012398 scopus 로고    scopus 로고
    • Chemokine receptors as HIV-1 coreceptors: Roles in viral entry, tropism, and disease
    • Berger, E. A., Murphy, P. M., Farber, J. M. (1999) Chemokine receptors as HIV-1 coreceptors: roles in viral entry, tropism, and disease Annu Rev Immunol 17, 657-700.
    • (1999) Annu Rev Immunol , vol.17 , pp. 657-700
    • Berger, E.A.1    Murphy, P.M.2    Farber, J.M.3
  • 9
    • 10944272588 scopus 로고    scopus 로고
    • Genetic control of retrovirus susceptibility in mammalian cells
    • Goff, S. P. (2004) Genetic control of retrovirus susceptibility in mammalian cells. Annu Rev Genet 38, 61-85.
    • (2004) Annu Rev Genet , vol.38 , pp. 61-85
    • Goff, S.P.1
  • 10
    • 33646193491 scopus 로고    scopus 로고
    • Dynamics of virus-host interplay in HIV-1 replication
    • Sorin, M., Kalpana, G. V. (2006) Dynamics of virus-host interplay in HIV-1 replication. Curr HIV Res 4, 117-30.
    • (2006) Curr HIV Res , vol.4 , pp. 117-130
    • Sorin, M.1    Kalpana, G.V.2
  • 11
    • 0038785584 scopus 로고    scopus 로고
    • Structural analyses of purified human immunodeficiency virus type 1 intracellular reverse transcription complexes
    • Nermut, M. V., Fassati, A. (2003) Structural analyses of purified human immunodeficiency virus type 1 intracellular reverse transcription complexes. J Virol 77, 8196-206.
    • (2003) J Virol , vol.77 , pp. 8196-8206
    • Nermut, M.V.1    Fassati, A.2
  • 12
    • 7444262816 scopus 로고    scopus 로고
    • A hard way to the nucleus
    • Bukrinsky, M. (2004) A hard way to the nucleus. Mol Med 10, 1-5.
    • (2004) Mol Med , vol.10 , pp. 1-5
    • Bukrinsky, M.1
  • 13
    • 32144445395 scopus 로고    scopus 로고
    • Intracytoplasmic maturation of the human immunodeficiency virus type 1 reverse transcription complexes determines their capacity to integrate into chromatin
    • Iordanskiy, S., Berro, R., Altieri, M., et al. (2006) Intracytoplasmic maturation of the human immunodeficiency virus type 1 reverse transcription complexes determines their capacity to integrate into chromatin. Retrovirology 3, 4.
    • (2006) Retrovirology , vol.3 , pp. 4
    • Iordanskiy, S.1    Berro, R.2    Altieri, M.3
  • 14
    • 0034973563 scopus 로고    scopus 로고
    • Cytoplasmic recruitment of INI1 and PML on incoming HIV preintegration complexes: Interference with early steps of viral replication
    • Turelli, P., Doucas, V., Craig, E., et al. (2001) Cytoplasmic recruitment of INI1 and PML on incoming HIV preintegration complexes: interference with early steps of viral replication. Mol Cell 7, 1245-54.
    • (2001) Mol Cell , vol.7 , pp. 1245-1254
    • Turelli, P.1    Doucas, V.2    Craig, E.3
  • 15
    • 33644831457 scopus 로고    scopus 로고
    • Biochemical and genetic analyses of integrase-interacting proteins lens epithelium-derived growth factor (LEDGF)/p75 and hepatoma-derived growth factor related protein 2 (HRP2) in preintegration complex function and HIV-1 replication
    • Vandegraaff, N., Devroe, E., Turlure, F., et al. (2006) Biochemical and genetic analyses of integrase-interacting proteins lens epithelium-derived growth factor (LEDGF)/p75 and hepatoma-derived growth factor related protein 2 (HRP2) in preintegration complex function and HIV-1 replication. Virology 346, 415-26.
    • (2006) Virology , vol.346 , pp. 415-426
    • Vandegraaff, N.1    Devroe, E.2    Turlure, F.3
  • 16
    • 33745745419 scopus 로고    scopus 로고
    • Retroviral DNA integration: HIV and the role of LEDGF/p75
    • Ciuffi, A., Bushman, F. D. (2006) Retroviral DNA integration: HIV and the role of LEDGF/p75. Trends Genet 22, 388-95.
    • (2006) Trends Genet , vol.22 , pp. 388-395
    • Ciuffi, A.1    Bushman, F.D.2
  • 17
    • 0032450548 scopus 로고    scopus 로고
    • HIV-1 Tat interacts with cyclin T1 to direct the P-TEFb CTD kinase complex to TAR RNA
    • Garber, M. E., Wei, P., Jones, K. A. (1998) HIV-1 Tat interacts with cyclin T1 to direct the P-TEFb CTD kinase complex to TAR RNA. Cold Spring Harb Symp Quant Biol 63, 371-80.
    • (1998) Cold Spring Harb Symp Quant Biol , vol.63 , pp. 371-380
    • Garber, M.E.1    Wei, P.2    Jones, K.A.3
  • 18
    • 0032548918 scopus 로고    scopus 로고
    • A novel CDK9-associated C-type cyclin interacts directly with HIV-1 Tat and mediates its high-affinity, loop-specific binding to TAR RNA
    • Wei, P., Garber, M. E., Fang, S. M., et al. (1998) A novel CDK9-associated C-type cyclin interacts directly with HIV-1 Tat and mediates its high-affinity, loop-specific binding to TAR RNA. Cell 92, 451-62.
    • (1998) Cell , vol.92 , pp. 451-462
    • Wei, P.1    Garber, M.E.2    Fang, S.M.3
  • 19
    • 33748190178 scopus 로고    scopus 로고
    • The integrase interactor 1 (INI1) proteins facilitate Tat-mediated human immunodeficiency virus type 1 transcription
    • Ariumi, Y., Serhan, F., Turelli, P., et al. (2006) The integrase interactor 1 (INI1) proteins facilitate Tat-mediated human immunodeficiency virus type 1 transcription. Retrovirology 3, 47.
    • (2006) Retrovirology , vol.3 , pp. 47
    • Ariumi, Y.1    Serhan, F.2    Turelli, P.3
  • 20
    • 0026729568 scopus 로고
    • Synergistic activation of the human immunodeficiency virus type 1 promoter by the viral Tat protein and cellular transcription factor Sp1
    • Kamine, J., Chinnadurai, G. (1992) Synergistic activation of the human immunodeficiency virus type 1 promoter by the viral Tat protein and cellular transcription factor Sp1. J Virol 66, 3932-6.
    • (1992) J Virol , vol.66 , pp. 3932-3936
    • Kamine, J.1    Chinnadurai, G.2
  • 21
    • 33746021681 scopus 로고    scopus 로고
    • The SWI/SNF chromatin-remodeling complex is a cofactor for Tat transactivation of the HIV promoter
    • Mahmoudi, T., Parra, M., Vries, R. G., et al. (2006) The SWI/SNF chromatin-remodeling complex is a cofactor for Tat transactivation of the HIV promoter. J Biol Chem 281, 19960-8.
    • (2006) J Biol Chem , vol.281 , pp. 19960-19968
    • Mahmoudi, T.1    Parra, M.2    Vries, R.G.3
  • 22
    • 34848881569 scopus 로고    scopus 로고
    • Transcriptional and post-transcriptional regulation of HIV-1 gene expression: Role of cellular factors for Tat and Rev
    • Nekhai, S., Jeang, K. T. (2006) Transcriptional and post-transcriptional regulation of HIV-1 gene expression: role of cellular factors for Tat and Rev. Future Microbiol 1, 417-26.
    • (2006) Future Microbiol , vol.1 , pp. 417-426
    • Nekhai, S.1    Jeang, K.T.2
  • 24
    • 17944363138 scopus 로고    scopus 로고
    • Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding
    • Garrus, J. E., von Schwedler, U. K., Pornillos, O. W., et al. (2001) Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding. Cell 107, 55-65.
    • (2001) Cell , vol.107 , pp. 55-65
    • Garrus, J.E.1    von Schwedler, U.K.2    Pornillos, O.W.3
  • 25
    • 0037011924 scopus 로고    scopus 로고
    • Identification of a host protein essential for assembly of immature HIV-1 capsids
    • Zimmerman, C., Klein, K. C., Kiser, P. K., et al. (2002) Identification of a host protein essential for assembly of immature HIV-1 capsids. Nature 415, 88-92.
    • (2002) Nature , vol.415 , pp. 88-92
    • Zimmerman, C.1    Klein, K.C.2    Kiser, P.K.3
  • 26
    • 36248936657 scopus 로고    scopus 로고
    • Beyond Tsg101: The role of Alix in 'ESCRTing' HIV-1
    • Fujii, K., Hurley, J. H., Freed, E. O. (2007) Beyond Tsg101: the role of Alix in 'ESCRTing' HIV-1. Nat Rev Microbiol 5, 912-6.
    • (2007) Nat Rev Microbiol , vol.5 , pp. 912-916
    • Fujii, K.1    Hurley, J.H.2    Freed, E.O.3
  • 27
    • 0025940629 scopus 로고
    • The two-hybrid system: A method to identify and clone genes for proteins that interact with a protein of interest
    • Chien, C. T., Bartel, P. L., Sternglanz, R., et al. (1991) The two-hybrid system: a method to identify and clone genes for proteins that interact with a protein of interest. Proc Natl Acad Sci U S A 88, 9578-82.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 9578-9582
    • Chien, C.T.1    Bartel, P.L.2    Sternglanz, R.3
  • 28
    • 0001200619 scopus 로고    scopus 로고
    • Bartel, P. L, and Fields, S, Eds, Oxford University Press, New York, NY
    • Chong, J. A., Mandel, G. (1997) in (Bartel, P. L., and Fields, S., Eds.), The Yeast Two-Hybrid System, pp. 289-97, Oxford University Press, New York, NY.
    • (1997) The Yeast Two-Hybrid System , pp. 289-297
    • Chong, J.A.1    Mandel, G.2
  • 29
    • 0029824170 scopus 로고    scopus 로고
    • A threehybrid system for detecting small ligandprotein receptor interactions
    • Licitra, E. J., Liu, J. O. (1996) A threehybrid system for detecting small ligandprotein receptor interactions. Proc Natl Acad Sci U S A 93, 12817-21.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 12817-12821
    • Licitra, E.J.1    Liu, J.O.2
  • 30
    • 0004975062 scopus 로고    scopus 로고
    • Bartel, P. L, and Fields, S, Eds, pp, Oxford University Press, New York, NY
    • Zhang, B., Kraemer, B., Sengupta, D., et al. (1997) in "The Yeast Two-Hybrid System" (Bartel, P. L., and Fields, S., Eds.), pp. 298-315, Oxford University Press, New York, NY.
    • (1997) The Yeast Two-Hybrid System , pp. 298-315
    • Zhang, B.1    Kraemer, B.2    Sengupta, D.3
  • 31
    • 0028802599 scopus 로고
    • The yeast tribrid system-genetic detection of trans-phosphorylated ITAMSH2-interactions
    • Osborne, M. A., Dalton, S., Kochan, J. P. (1995) The yeast tribrid system-genetic detection of trans-phosphorylated ITAMSH2-interactions. Biotechnology (N Y) 13, 1474-8.
    • (1995) Biotechnology (N Y) , vol.13 , pp. 1474-1478
    • Osborne, M.A.1    Dalton, S.2    Kochan, J.P.3
  • 32
    • 0030761092 scopus 로고    scopus 로고
    • A conditionally expressed third partner stabilizes or prevents the formation of a transcriptional activator in a three-hybrid system
    • Tirode, F., Malaguti, C., Romero, F., et al. (1997) A conditionally expressed third partner stabilizes or prevents the formation of a transcriptional activator in a three-hybrid system. J Biol Chem 272, 22995-9.
    • (1997) J Biol Chem , vol.272 , pp. 22995-22999
    • Tirode, F.1    Malaguti, C.2    Romero, F.3
  • 33
    • 0028786569 scopus 로고
    • Yeast two-hybrid system demonstrates that estrogen receptor dimerization is ligand-dependent in vivo
    • Wang, H., Peters, G. A., Zeng, X., et al. (1995) Yeast two-hybrid system demonstrates that estrogen receptor dimerization is ligand-dependent in vivo. J Biol Chem 270, 23322-9.
    • (1995) J Biol Chem , vol.270 , pp. 23322-23329
    • Wang, H.1    Peters, G.A.2    Zeng, X.3
  • 34
    • 0029809862 scopus 로고    scopus 로고
    • Reverse two-hybrid and onehybrid systems to detect dissociation of protein-protein and DNA-protein interactions
    • Vidal, M., Brachmann, R. K., Fattaey, A., et al. (1996) Reverse two-hybrid and onehybrid systems to detect dissociation of protein-protein and DNA-protein interactions. Proc Natl Acad Sci U S A 93, 10315-20.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 10315-10320
    • Vidal, M.1    Brachmann, R.K.2    Fattaey, A.3
  • 35
    • 0035478339 scopus 로고    scopus 로고
    • Humoral immune response directed against LEDGF in patients with VKH
    • Yamada, K., Senju, S., Shinohara, T., et al. (2001) Humoral immune response directed against LEDGF in patients with VKH. Immunol Lett 78, 161-8.
    • (2001) Immunol Lett , vol.78 , pp. 161-168
    • Yamada, K.1    Senju, S.2    Shinohara, T.3
  • 37
    • 0032963671 scopus 로고    scopus 로고
    • c-MYC interacts with INI1/hSNF5 and requires the SWI/SNF complex for transactivation function
    • Cheng, S. W., Davies, K. P., Yung, E., et al. (1999) c-MYC interacts with INI1/hSNF5 and requires the SWI/SNF complex for transactivation function. Nat. Genet. 22, 102-5.
    • (1999) Nat. Genet , vol.22 , pp. 102-105
    • Cheng, S.W.1    Davies, K.P.2    Yung, E.3
  • 38
    • 0033519709 scopus 로고    scopus 로고
    • Interaction of E1 and hSNF5 proteins stimulates replication of human papillomavirus DNA
    • Lee, D., Sohn, H., Kalpana, G. V., et al. (1999) Interaction of E1 and hSNF5 proteins stimulates replication of human papillomavirus DNA. Nature 399, 487-91.
    • (1999) Nature , vol.399 , pp. 487-491
    • Lee, D.1    Sohn, H.2    Kalpana, G.V.3
  • 39
    • 0032477738 scopus 로고    scopus 로고
    • Structure-function analysis of integrase interactor 1/hSNF5L1 reveals differential properties of two repeat motifs present in the highly conserved region
    • Morozov A, Y. E., Kalpana GV (1998) Structure-function analysis of integrase interactor 1/hSNF5L1 reveals differential properties of two repeat motifs present in the highly conserved region. Proc Natl Acad Sci U S A 95, 1120-5.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 1120-1125
    • Morozov, A.Y.E.1    Kalpana, G.V.2
  • 40
    • 0034885519 scopus 로고    scopus 로고
    • Inhibition of HIV-1 virion production by a transdominant mutant of integrase interactor 1
    • Yung, E., Sorin, M., Pal, A., et al. (2001) Inhibition of HIV-1 virion production by a transdominant mutant of integrase interactor 1. Nat Med 7, 920-6.
    • (2001) Nat Med , vol.7 , pp. 920-926
    • Yung, E.1    Sorin, M.2    Pal, A.3
  • 41
    • 0033526768 scopus 로고    scopus 로고
    • Isolation and characterization of an oligomerization-negative mutant of HIV-1 integrase
    • Kalpana, G. V., Reicin, A., Cheng, G. S., et al. (1999) Isolation and characterization of an oligomerization-negative mutant of HIV-1 integrase. Virology 259, 274-85.
    • (1999) Virology , vol.259 , pp. 274-285
    • Kalpana, G.V.1    Reicin, A.2    Cheng, G.S.3
  • 42
    • 27644576841 scopus 로고    scopus 로고
    • High-throughput two-hybrid analysis. The promise and the peril
    • Fields, S. (2005) High-throughput two-hybrid analysis. The promise and the peril. Febs J 272, 5391-9.
    • (2005) Febs J , vol.272 , pp. 5391-5399
    • Fields, S.1
  • 43
    • 9044231763 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1Vpr protein binds to the uracil DNA glycosylase DNA repair enzyme
    • Bouhamdan, M., Benichou, S., Rey, F., et al. (1996) Human immunodeficiency virus type 1Vpr protein binds to the uracil DNA glycosylase DNA repair enzyme J Virol 70, 697-704.
    • (1996) J Virol , vol.70 , pp. 697-704
    • Bouhamdan, M.1    Benichou, S.2    Rey, F.3
  • 44
    • 0004270170 scopus 로고
    • Ausubel, F. M, Brent, R, Kingston, R. E, Moore, D. D, Seidman, J. G, Smith, J. A, and Struhl, K, eds, John Wiley and Sons
    • Engebrecht, J., Brent, R., Kaderbhai, M. A. (1991) in (Ausubel, F. M., Brent, R., Kingston, R. E., Moore, D. D., Seidman, J. G., Smith, J. A., and Struhl, K., eds.), Current Protocols in Molecular Biology, John Wiley and Sons.
    • (1991) Current Protocols in Molecular Biology
    • Engebrecht, J.1    Brent, R.2    Kaderbhai, M.A.3
  • 45
    • 60349098352 scopus 로고    scopus 로고
    • Scopes, R. K., Smith, J. A. (2006) in (Ausbel, F. M., Brent, R., Kingston, R. E., Moore, D. D., Seidman, J. G., Smith, J. A., and Struhl, K., eds.), Current Protocols in Molecular Biology, pp. 10.0.1, John Wiley and Sons, Inc.
    • Scopes, R. K., Smith, J. A. (2006) in (Ausbel, F. M., Brent, R., Kingston, R. E., Moore, D. D., Seidman, J. G., Smith, J. A., and Struhl, K., eds.), Current Protocols in Molecular Biology, pp. 10.0.1, John Wiley and Sons, Inc.


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