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Volumn 86, Issue 1, 2012, Pages 513-526

Stimulation of the human RAD51 nucleofilament restricts HIV-1 integration in vitro and in infected cells

Author keywords

[No Author keywords available]

Indexed keywords

3 [(BENZYLAMINO)SULFONYL] 4 BROMO N (4 BROMOPHENYL)BENZAMIDE; ACTIN BINDING PROTEIN; ANTIVIRUS AGENT; INTEGRASE; NUCLEOFILAMENT; RAD51 PROTEIN; RS 1; UNCLASSIFIED DRUG;

EID: 84855931884     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.05425-11     Document Type: Article
Times cited : (28)

References (44)
  • 1
    • 0035964292 scopus 로고    scopus 로고
    • DNA aptamers selected against the HIV-1 RNase H display in vitro antiviral activity
    • Andreola ML, et al. 2001. DNA aptamers selected against the HIV-1 RNase H display in vitro antiviral activity. Biochemistry 40:10087-10094.
    • (2001) Biochemistry , vol.40 , pp. 10087-10094
    • Andreola, M.L.1
  • 2
    • 0038136948 scopus 로고    scopus 로고
    • Contribution of DNA conformation and topology in right-handed DNA wrapping by the Bacillus subtilis LrpC protein
    • Beloin C, et al. 2003. Contribution of DNA conformation and topology in right-handed DNA wrapping by the Bacillus subtilis LrpC protein. J. Biol. Chem. 278:5333-5342.
    • (2003) J. Biol. Chem. , vol.278 , pp. 5333-5342
    • Beloin, C.1
  • 3
    • 0034671528 scopus 로고    scopus 로고
    • Modeling the late steps in HIV-1 retroviral integrase-catalyzed DNA integration
    • Brin E, Yi J, Skalka AM, Leis J. 2000. Modeling the late steps in HIV-1 retroviral integrase-catalyzed DNA integration. J. Biol. Chem. 275: 39287-39295.
    • (2000) J. Biol. Chem. , vol.275 , pp. 39287-39295
    • Brin, E.1    Yi, J.2    Skalka, A.M.3    Leis, J.4
  • 4
    • 0242499964 scopus 로고    scopus 로고
    • Longitudinal monitoring of 2-long terminal repeat circles in peripheral blood mononuclear cells from patients with chronic HIV-1 infection
    • Brussel A, et al. 2003. Longitudinal monitoring of 2-long terminal repeat circles in peripheral blood mononuclear cells from patients with chronic HIV-1 infection. AIDS 17:645- 652.
    • (2003) AIDS , vol.17 , pp. 645-652
    • Brussel, A.1
  • 5
    • 0141457701 scopus 로고    scopus 로고
    • Analysis of early human immunodeficiency virus type 1 DNA synthesis by use of a new sensitive assay for quantifying integrated provirus
    • Brussel A, Sonigo P. 2003. Analysis of early human immunodeficiency virus type 1 DNA synthesis by use of a new sensitive assay for quantifying integrated provirus. J. Virol. 77:10119 -10124.
    • (2003) J. Virol. , vol.77 , pp. 10119-10124
    • Brussel, A.1    Sonigo, P.2
  • 6
    • 32644466860 scopus 로고    scopus 로고
    • Roles of ATP binding and ATP hydrolysis in human Rad51 recombinase function
    • Chi P, Van Komen S, Sehorn MG, Sigurdsson S, Sung P. 2006. Roles of ATP binding and ATP hydrolysis in human Rad51 recombinase function. DNA Repair (Amst) 5:381-391.
    • (2006) DNA Repair (Amst) , vol.5 , pp. 381-391
    • Chi, P.1    Van Komen, S.2    Sehorn, M.G.3    Sigurdsson, S.4    Sung, P.5
  • 7
    • 33646355164 scopus 로고    scopus 로고
    • Cooperativity between Rad51 and C/EBP family transcription factors modulates basal and Tat-induced activation of the HIV-1 LTR in astrocytes
    • Chipitsyna G, Sawaya BE, Khalili K, Amini S. 2006. Cooperativity between Rad51 and C/EBP family transcription factors modulates basal and Tat-induced activation of the HIV-1 LTR in astrocytes. J. Cell. Physiol. 207:605- 613.
    • (2006) J. Cell. Physiol. , vol.207 , pp. 605-613
    • Chipitsyna, G.1    Sawaya, B.E.2    Khalili, K.3    Amini, S.4
  • 8
    • 0028012053 scopus 로고
    • Fusion from without directed by human immunodeficiency virus particles
    • Clavel F, Charneau P. 1994. Fusion from without directed by human immunodeficiency virus particles. J. Virol. 68:1179 -1185.
    • (1994) J. Virol. , vol.68 , pp. 1179-1185
    • Clavel, F.1    Charneau, P.2
  • 9
    • 0035141303 scopus 로고    scopus 로고
    • Wortmannin potentiates integrase-mediated killing of lymphocytes and reduces the efficiency of stable transduction by retroviruses
    • Daniel R, et al. 2001. Wortmannin potentiates integrase-mediated killing of lymphocytes and reduces the efficiency of stable transduction by retroviruses. Mol. Cell. Biol. 21:1164 -1172.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 1164-1172
    • Daniel, R.1
  • 10
    • 0033597450 scopus 로고    scopus 로고
    • A role for DNA-PK in retroviral DNA integration
    • Daniel R, Katz RA, Skalka AM. 1999. A role for DNA-PK in retroviral DNA integration. Science 284:644-647.
    • (1999) Science , vol.284 , pp. 644-647
    • Daniel, R.1    Katz, R.A.2    Skalka, A.M.3
  • 11
    • 8544226285 scopus 로고    scopus 로고
    • Histone H2AX is phosphorylated at sites of retroviralDNAintegration but is dispensable for postintegration repair
    • Daniel R, et al. 2004. Histone H2AX is phosphorylated at sites of retroviralDNAintegration but is dispensable for postintegration repair. J. Biol. Chem. 279:45810-45814.
    • (2004) J. Biol. Chem. , vol.279 , pp. 45810-45814
    • Daniel, R.1
  • 12
    • 33845643161 scopus 로고    scopus 로고
    • Chromosomal integration of LTR-flanked DNA in yeast expressing HIV-1 integrase: down regulation by RAD51
    • Desfarges S, et al. 2006. Chromosomal integration of LTR-flanked DNA in yeast expressing HIV-1 integrase: down regulation by RAD51. Nucleic Acids Res. 34:6215- 6224.
    • (2006) Nucleic Acids Res , vol.34 , pp. 6215-6224
    • Desfarges, S.1
  • 13
    • 56149096153 scopus 로고    scopus 로고
    • Rad51 polymerization reveals a new chromatin remodeling mechanism
    • Dupaigne P, et al. 2008. Rad51 polymerization reveals a new chromatin remodeling mechanism. PLoS One 3:e3643.
    • (2008) PLoS One , vol.3
    • Dupaigne, P.1
  • 14
    • 79952949357 scopus 로고    scopus 로고
    • siRNA screening of a targeted library of DNA repair factors in HIV infection reveals a role for base excision repair in HIV integration
    • Espeseth AS, et al. 2011. siRNA screening of a targeted library of DNA repair factors in HIV infection reveals a role for base excision repair in HIV integration. PLoS One 6:e17612.
    • (2011) PLoS One , vol.6
    • Espeseth, A.S.1
  • 15
    • 77949365510 scopus 로고    scopus 로고
    • Retroviral intasome assembly and inhibition of DNA strand transfer
    • Hare S, Gupta SS, Valkov E, Engelman A, Cherepanov P. 2010. Retroviral intasome assembly and inhibition of DNA strand transfer. Nature 464:232-236.
    • (2010) Nature , vol.464 , pp. 232-236
    • Hare, S.1    Gupta, S.S.2    Valkov, E.3    Engelman, A.4    Cherepanov, P.5
  • 16
    • 0036199768 scopus 로고    scopus 로고
    • Improved primate foamy virus vectors and packaging constructs
    • Heinkelein M, et al. 2002. Improved primate foamy virus vectors and packaging constructs. J. Virol. 76:3774 -3783.
    • (2002) J. Virol. , vol.76 , pp. 3774-3783
    • Heinkelein, M.1
  • 18
    • 57349128865 scopus 로고    scopus 로고
    • A chemical compound that stimulates the human homologous recombination protein RAD51
    • Jayathilaka K, et al. 2008. A chemical compound that stimulates the human homologous recombination protein RAD51. Proc. Natl. Acad. Sci. U. S. A. 105:15848 -15853.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 15848-15853
    • Jayathilaka, K.1
  • 19
    • 0141792085 scopus 로고    scopus 로고
    • Roles of host cell factors in circularization of retroviral dna
    • Kilzer JM, et al. 2003. Roles of host cell factors in circularization of retroviral dna. Virology 314:460-467.
    • (2003) Virology , vol.314 , pp. 460-467
    • Kilzer, J.M.1
  • 20
    • 42249115685 scopus 로고    scopus 로고
    • The consequences of Rad51 overexpression for normal and tumor cells
    • Klein HL. 2008. The consequences of Rad51 overexpression for normal and tumor cells. DNA Repair (Amst) 7:686-693.
    • (2008) DNA Repair (Amst) , vol.7 , pp. 686-693
    • Klein, H.L.1
  • 21
    • 77957670046 scopus 로고    scopus 로고
    • Structure-based modeling of the functional HIV-1 intasome and its inhibition
    • Krishnan L, et al. 2010. Structure-based modeling of the functional HIV-1 intasome and its inhibition. Proc. Natl. Acad. Sci. U. S. A. 107: 15910-15915.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 15910-15915
    • Krishnan, L.1
  • 22
    • 4444363150 scopus 로고    scopus 로고
    • Suppression of retroviral infection by the RAD52 DNA repair protein
    • Lau A, Kanaar R, Jackson SP, O'Connor MJ. 2004. Suppression of retroviral infection by the RAD52 DNA repair protein. EMBO J. 23: 3421-3429.
    • (2004) EMBO J , vol.23 , pp. 3421-3429
    • Lau, A.1    Kanaar, R.2    Jackson, S.P.3    O'Connor, M.J.4
  • 23
    • 79952205472 scopus 로고    scopus 로고
    • Functional coupling between HIV-1 integrase and the SWI/SNF chromatin remodeling complex for efficient in vitro integration into stable nucleosomes
    • Lesbats P, et al. 2011. Functional coupling between HIV-1 integrase and the SWI/SNF chromatin remodeling complex for efficient in vitro integration into stable nucleosomes. PLoS Pathog. 7:e1001280.
    • (2011) PLoS Pathog , vol.7
    • Lesbats, P.1
  • 24
    • 58149493911 scopus 로고    scopus 로고
    • In vitro initial attachment of HIV-1 integrase to viral ends: control of the DNA specific interaction by the oligomerization state
    • Lesbats P, et al. 2008. In vitro initial attachment of HIV-1 integrase to viral ends: control of the DNA specific interaction by the oligomerization state. Nucleic Acids Res. 36:7043-7058.
    • (2008) Nucleic Acids Res , vol.36 , pp. 7043-7058
    • Lesbats, P.1
  • 25
    • 0028863006 scopus 로고
    • Disassembly of the Mu transposase tetramer by the ClpX chaperone
    • Levchenko I, Luo L, Baker TA. 1995. Disassembly of the Mu transposase tetramer by the ClpX chaperone. Genes Dev. 9:2399-2408.
    • (1995) Genes Dev , vol.9 , pp. 2399-2408
    • Levchenko, I.1    Luo, L.2    Baker, T.A.3
  • 26
    • 0035876374 scopus 로고    scopus 로고
    • Role of the non-homologous DNA end joining pathway in the early steps of retroviral infection
    • Li L, et al. 2001. Role of the non-homologous DNA end joining pathway in the early steps of retroviral infection. EMBO J. 20:3272-3281.
    • (2001) EMBO J , vol.20 , pp. 3272-3281
    • Li, L.1
  • 27
    • 33646943507 scopus 로고    scopus 로고
    • Effect of DNA repair protein Rad18 on viral infection
    • Lloyd AG, et al. 2006. Effect of DNA repair protein Rad18 on viral infection. PLoS Pathog. 2:e40.
    • (2006) PLoS Pathog , vol.2
    • Lloyd, A.G.1
  • 28
    • 78149434355 scopus 로고    scopus 로고
    • The mechanism of retroviral integration from X-ray structures of its key intermediates
    • Maertens GN, Hare S, Cherepanov P. 2010. The mechanism of retroviral integration from X-ray structures of its key intermediates. Nature 468: 326-329.
    • (2010) Nature , vol.468 , pp. 326-329
    • Maertens, G.N.1    Hare, S.2    Cherepanov, P.3
  • 29
    • 34547143223 scopus 로고    scopus 로고
    • Cellular uptake of ODNs in HIV-1 humaninfected cells: a role for viral particles in DNA delivery?
    • Metifiot M, et al. 2007. Cellular uptake of ODNs in HIV-1 humaninfected cells: a role for viral particles in DNA delivery? Oligonucleotides 17:151-165.
    • (2007) Oligonucleotides , vol.17 , pp. 151-165
    • Metifiot, M.1
  • 30
    • 34748827049 scopus 로고    scopus 로고
    • von Hippel Lindau binding protein 1-mediated degradation of integrase affects HIV-1 gene expression at a postintegration step
    • Mousnier A, et al. 2007. von Hippel Lindau binding protein 1-mediated degradation of integrase affects HIV-1 gene expression at a postintegration step. Proc. Natl. Acad. Sci. U. S. A. 104:13615-13620.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 13615-13620
    • Mousnier, A.1
  • 31
    • 0037178886 scopus 로고    scopus 로고
    • Interaction of HIV-1 integrase with DNA repair protein hRad18
    • Mulder LC, Chakrabarti LA, Muesing MA. 2002. Interaction of HIV-1 integrase with DNA repair protein hRad18. J. Biol. Chem. 277: 27489-27493.
    • (2002) J. Biol. Chem. , vol.277 , pp. 27489-27493
    • Mulder, L.C.1    Chakrabarti, L.A.2    Muesing, M.A.3
  • 32
    • 80052494157 scopus 로고    scopus 로고
    • Prototype foamy virus Gag nuclear localization: a novel pathway among retroviruses
    • Mullers E, Stirnnagel K, Kaulfuss S, Lindemann D. 2011. Prototype foamy virus Gag nuclear localization: a novel pathway among retroviruses. J. Virol. 85:9276 -9285.
    • (2011) J. Virol. , vol.85 , pp. 9276-9285
    • Mullers, E.1    Stirnnagel, K.2    Kaulfuss, S.3    Lindemann, D.4
  • 33
    • 10744232511 scopus 로고    scopus 로고
    • The lethal phenotype observed after HIV-1 integrase expression in yeast cells is related to DNA repair and recombination events
    • Parissi V, et al. 2003. The lethal phenotype observed after HIV-1 integrase expression in yeast cells is related to DNA repair and recombination events. Gene 322:157-168.
    • (2003) Gene , vol.322 , pp. 157-168
    • Parissi, V.1
  • 34
    • 0037364872 scopus 로고    scopus 로고
    • Comparison of the sulforhodamine B assay and the clonogenic assay for in vitro chemoradiation studies
    • Pauwels B, et al. 2003. Comparison of the sulforhodamine B assay and the clonogenic assay for in vitro chemoradiation studies. Cancer Chemother. Pharmacol. 51:221-226.
    • (2003) Cancer Chemother. Pharmacol. , vol.51 , pp. 221-226
    • Pauwels, B.1
  • 35
    • 77956985497 scopus 로고    scopus 로고
    • Activation of HIV-1 LTR by Rad51 in microglial cells
    • Rom I, et al. 2010. Activation of HIV-1 LTR by Rad51 in microglial cells. Cell Cycle 9:3715-3722.
    • (2010) Cell Cycle , vol.9 , pp. 3715-3722
    • Rom, I.1
  • 36
    • 0024443881 scopus 로고
    • Human immunodeficiency virus reverse transcriptase expressed in transformed yeast cells. Biochemical properties and interactions with bovine tRNALys
    • Sallafranque-Andreola ML, et al. 1989. Human immunodeficiency virus reverse transcriptase expressed in transformed yeast cells. Biochemical properties and interactions with bovine tRNALys. Eur. J. Biochem. 184: 367-374.
    • (1989) Eur. J. Biochem. , vol.184 , pp. 367-374
    • Sallafranque-Andreola, M.L.1
  • 37
    • 50649100744 scopus 로고    scopus 로고
    • Mechanism of eukaryotic homologous recombination
    • San Filippo J, Sung P, Klein H. 2008. Mechanism of eukaryotic homologous recombination. Annu. Rev. Biochem. 77:229 -257.
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 229-257
    • San Filippo, J.1    Sung, P.2    Klein, H.3
  • 38
    • 77952222409 scopus 로고    scopus 로고
    • Analysis of prototype foamy virus particle-host cell interaction with autofluorescent retroviral particles
    • Stirnnagel K, et al. 2010. Analysis of prototype foamy virus particle-host cell interaction with autofluorescent retroviral particles. Retrovirology 7:45.
    • (2010) Retrovirology , vol.7 , pp. 45
    • Stirnnagel, K.1
  • 39
    • 33749037701 scopus 로고    scopus 로고
    • Mechanism of homologous recombination: mediators and helicases take on regulatory functions
    • Sung P, Klein H. 2006. Mechanism of homologous recombination: mediators and helicases take on regulatory functions. Nat. Rev. Mol. Cell Biol. 7:739 -750.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 739-750
    • Sung, P.1    Klein, H.2
  • 40
    • 4444225676 scopus 로고    scopus 로고
    • Mutational analyses of the human Rad51-Tyr315 residue, a site for phosphorylation in leukaemia cells
    • Takizawa Y, et al. 2004. Mutational analyses of the human Rad51-Tyr315 residue, a site for phosphorylation in leukaemia cells. Genes Cells 9:781-790.
    • (2004) Genes Cells , vol.9 , pp. 781-790
    • Takizawa, Y.1
  • 41
    • 58549092798 scopus 로고    scopus 로고
    • Functional and structural characterization of the integrase from the prototype foamy virus
    • Valkov E, et al. 2009. Functional and structural characterization of the integrase from the prototype foamy virus. Nucleic Acids Res. 37:243-255.
    • (2009) Nucleic Acids Res , vol.37 , pp. 243-255
    • Valkov, E.1
  • 42
    • 0029643952 scopus 로고
    • Recombining the structures of HIV integrase, RuvC and RNase H
    • Yang W, Steitz TA. 1995. Recombining the structures of HIV integrase, RuvC and RNase H. Structure 3:131-134.
    • (1995) Structure , vol.3 , pp. 131-134
    • Yang, W.1    Steitz, T.A.2
  • 43
    • 0034468560 scopus 로고    scopus 로고
    • Repair of gaps in retroviral DNA integration intermediates
    • Yoder KE, Bushman FD. 2000. Repair of gaps in retroviral DNA integration intermediates. J. Virol. 74:11191-11200.
    • (2000) J. Virol. , vol.74 , pp. 11191-11200
    • Yoder, K.E.1    Bushman, F.D.2
  • 44
    • 79952957934 scopus 로고    scopus 로고
    • The base excision repair pathway is required for efficient lentivirus integration
    • Yoder KE, et al. 2011. The base excision repair pathway is required for efficient lentivirus integration. PLoS One 6:e17862.
    • (2011) PLoS One , vol.6
    • Yoder, K.E.1


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