메뉴 건너뛰기




Volumn 36, Issue 10, 2004, Pages 1099-1104

The EBV lytic switch protein, Z, preferentially binds to and activates the methylated viral genome

Author keywords

[No Author keywords available]

Indexed keywords

FATTY ACID BINDING PROTEIN; TRANSCRIPTION FACTOR; BZLF2 PROTEIN, HERPESVIRUS 4, HUMAN; GLYCOPROTEIN; VIRUS DNA; VIRUS PROTEIN;

EID: 6944244957     PISSN: 10614036     EISSN: None     Source Type: Journal    
DOI: 10.1038/ng1424     Document Type: Article
Times cited : (161)

References (30)
  • 1
    • 0000942113 scopus 로고    scopus 로고
    • Epstein-Barr virus
    • (eds. B.N. Fields et al.) (Lippincott-Raven, Philadelphia)
    • rd edn. (eds. B.N. Fields et al.) 2397-2446 (Lippincott-Raven, Philadelphia, 1996).
    • (1996) rd Edn. , pp. 2397-2446
    • Rickinson, A.B.1    Kieff, E.2
  • 2
    • 0000942113 scopus 로고    scopus 로고
    • Epstein-Barr virus and its replication
    • (eds. B.N. Fields et al.) (Lippincott-Raven, Philadelphia)
    • rd edn. (eds. B.N. Fields et al.) 2343-2396 (Lippincott-Raven, Philadelphia, 1996).
    • (1996) rd Edn. , pp. 2343-2396
    • Kieff, E.1
  • 3
    • 0023036072 scopus 로고
    • Both Epstein-Barr virus (EBV) encoded transacting factors, EB1 and EB2, are required to activate transcription from an early EBV promoter
    • Chevallier-Greco, A. et al. Both Epstein-Barr virus (EBV) encoded transacting factors, EB1 and EB2, are required to activate transcription from an early EBV promoter. EMBO J. 5, 3243-3249 (1986).
    • (1986) EMBO J. , vol.5 , pp. 3243-3249
    • Chevallier-Greco, A.1
  • 4
    • 1642457437 scopus 로고
    • Activation of expression of latent Epstein-Barr virus after gene transfer with a small cloned fragment of heterogeneous viral DNA
    • Countryman, J. & Miller, G. Activation of expression of latent Epstein-Barr virus after gene transfer with a small cloned fragment of heterogeneous viral DNA. Proc. Natl. Acad. Sci. USA 82, 4085-4089 (1985).
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 4085-4089
    • Countryman, J.1    Miller, G.2
  • 5
    • 0022646563 scopus 로고
    • Transactivation of the latent Epstein-Barr virus genome after transfection of the EBV DNA fragment
    • Takada, K., Shimizu, N., Sakuma, S. & Ono, Y. Transactivation of the latent Epstein-Barr virus genome after transfection of the EBV DNA fragment. J. Virol. 57, 1016-1022 (1986).
    • (1986) J. Virol. , vol.57 , pp. 1016-1022
    • Takada, K.1    Shimizu, N.2    Sakuma, S.3    Ono, Y.4
  • 6
    • 0029830047 scopus 로고    scopus 로고
    • Epstein-Barr viral latency is disrupted by the immediate-early BRLF1 protein through a cell-specific mechanism
    • Zalani, S., Holley-Guthrie, E. & Kenney, S. Epstein-Barr viral latency is disrupted by the immediate-early BRLF1 protein through a cell-specific mechanism. Proc. Natl. Acad. Sci. USA 93, 9194-9199 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9194-9199
    • Zalani, S.1    Holley-Guthrie, E.2    Kenney, S.3
  • 7
    • 0031694397 scopus 로고    scopus 로고
    • The Epstein-Barr virus Rta protein disrupts latency in B lymphocytes
    • Ragoczy, T., Heston, L. & Miller, G. The Epstein-Barr virus Rta protein disrupts latency in B lymphocytes. J. Virol. 72, 7978-7984 (1998).
    • (1998) J. Virol. , vol.72 , pp. 7978-7984
    • Ragoczy, T.1    Heston, L.2    Miller, G.3
  • 8
    • 0024469056 scopus 로고
    • Epstein-Barr virus BZLF1 transactivator specifically binds to consensus AP-1 site and is related to c-fos
    • Farrell, P., Rowe, D., Rooney, C. & Kouzarides, T. Epstein-Barr virus BZLF1 transactivator specifically binds to consensus AP-1 site and is related to c-fos. EMBO J. 8, 127-132 (1989).
    • (1989) EMBO J. , vol.8 , pp. 127-132
    • Farrell, P.1    Rowe, D.2    Rooney, C.3    Kouzarides, T.4
  • 9
    • 0025290086 scopus 로고
    • The Epstein-Barr virus Zta transactivator: A member of bZIP family with unique DNA-binding specificity and a dimerization domainthat lacks the characteristic heptad leucine zipper motif
    • Chang, Y., Dong, D., Hayward, G. & Hayward, S.D. The Epstein-Barr virus Zta transactivator: a member of bZIP family with unique DNA-binding specificity and a dimerization domainthat lacks the characteristic heptad leucine zipper motif. J. Virol. 64, 3358-3369 (1990).
    • (1990) J. Virol. , vol.64 , pp. 3358-3369
    • Chang, Y.1    Dong, D.2    Hayward, G.3    Hayward, S.D.4
  • 10
    • 0025604607 scopus 로고
    • Evidence for coited-coil dimmer formation by an Epstein-Barr virus transactivator that lacks a heptad repeat of leucine residues
    • Flemington, E. & Speck, S. Evidence for coited-coil dimmer formation by an Epstein-Barr virus transactivator that lacks a heptad repeat of leucine residues. Proc. Natl. Acad. Sci. USA 87, 9459-9463 (1991).
    • (1991) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 9459-9463
    • Flemington, E.1    Speck, S.2
  • 11
    • 0032506210 scopus 로고    scopus 로고
    • Rescue of the Epstein-Barr virus BZLF1 mutant, Z(S186A), early gene activation defect by the BRLF1 gene product
    • Adamson, A. & Kenney, S.C. Rescue of the Epstein-Barr virus BZLF1 mutant, Z(S186A), early gene activation defect by the BRLF1 gene product. Virology 251, 187-197 (1998).
    • (1998) Virology , vol.251 , pp. 187-197
    • Adamson, A.1    Kenney, S.C.2
  • 12
    • 0034660443 scopus 로고    scopus 로고
    • The Epstein-Barr virus lytic program is controlled by the co-operative functions of two transactivators
    • Feederle, R. et al. The Epstein-Barr virus lytic program is controlled by the co-operative functions of two transactivators. EMBO J. 19, 3080-3089 (2000).
    • (2000) EMBO J. , vol.19 , pp. 3080-3089
    • Feederle, R.1
  • 13
    • 0025265593 scopus 로고
    • Structure and function of the Epstein-Barr virus BZLF1 protein
    • Packham, G., Economou, A., Rooney, C.M., Rowe, D. & Farrell, P.J. Structure and function of the Epstein-Barr virus BZLF1 protein. J. Virol. 64, 2110-2116 (1990).
    • (1990) J. Virol. , vol.64 , pp. 2110-2116
    • Packham, G.1    Economou, A.2    Rooney, C.M.3    Rowe, D.4    Farrell, P.J.5
  • 14
    • 0035026624 scopus 로고    scopus 로고
    • Autostimulation of the Epstein-Barr virus BRLF1 promoter is mediated through consensus Sp1 and Sp3 binding sites
    • Ragoczy, T. & Miller, G. Autostimulation of the Epstein-Barr virus BRLF1 promoter is mediated through consensus Sp1 and Sp3 binding sites. J. Virol. 75, 5240-5251 (2001).
    • (2001) J. Virol. , vol.75 , pp. 5240-5251
    • Ragoczy, T.1    Miller, G.2
  • 15
    • 0033982336 scopus 로고    scopus 로고
    • Epstein-Barr virus immediate-early proteins BZLF1 and BRLF1 activate the ATF2 transcription factor by increasing the levels of phosphorylated p38 and c-Jun N-terminal kinases
    • Adamson, A.L. et al. Epstein-Barr virus immediate-early proteins BZLF1 and BRLF1 activate the ATF2 transcription factor by increasing the levels of phosphorylated p38 and c-Jun N-terminal kinases. J. Virol. 74, 1224-1233 (2000).
    • (2000) J. Virol. , vol.74 , pp. 1224-1233
    • Adamson, A.L.1
  • 16
    • 0037068372 scopus 로고    scopus 로고
    • DNA methylation and chromatin- unraveling the tangled web
    • Robertson, K. DNA methylation and chromatin- unraveling the tangled web. Oncogene 21, 5361-5379 (2002).
    • (2002) Oncogene , vol.21 , pp. 5361-5379
    • Robertson, K.1
  • 17
    • 0033753779 scopus 로고    scopus 로고
    • The DNA methyltransferases of mammals
    • Bestor, T.H. The DNA methyltransferases of mammals. Hum. Mol. Genet. 9, 2395-2402 (2000).
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2395-2402
    • Bestor, T.H.1
  • 18
    • 0024458683 scopus 로고
    • The role of methylation in the phenotype-dependent modulation of Epstein-Barr nuclear antigen 2 and latent membrane protein genes in cells latently infected with Epstein-Barr virus
    • Ernberg, I. et al. The role of methylation in the phenotype-dependent modulation of Epstein-Barr nuclear antigen 2 and latent membrane protein genes in cells latently infected with Epstein-Barr virus. J. Gen. Virol. 70, 2989-3002 (1989).
    • (1989) J. Gen. Virol. , vol.70 , pp. 2989-3002
    • Ernberg, I.1
  • 19
    • 0032752850 scopus 로고    scopus 로고
    • Differential methylation of Epstein-Barr virus latency promoters facilitates viral persistence in healthy seropositive individuals
    • Paulson, E.J. & Speck, S.H. Differential methylation of Epstein-Barr virus latency promoters facilitates viral persistence in healthy seropositive individuals. J. Virol. 73, 9959-9968 (1999).
    • (1999) J. Virol. , vol.73 , pp. 9959-9968
    • Paulson, E.J.1    Speck, S.H.2
  • 20
    • 0030689030 scopus 로고    scopus 로고
    • Methylation of the Epstein-Barr virus genome in normal lymphocytes
    • Robertson, K.D. & Ambinder, R.F. Methylation of the Epstein-Barr virus genome in normal lymphocytes. Blood 90, 4480-4484 (1997).
    • (1997) Blood , vol.90 , pp. 4480-4484
    • Robertson, K.D.1    Ambinder, R.F.2
  • 21
    • 0024381772 scopus 로고
    • 5-Azacytidine up regulates the expression of Epstein-Barr virus nuclear antigen 2 (EBNA-2) through EBNA-6 and latent membrane protein in the Burkitt's lymphoma line rael
    • Masucci, M.G. et al. 5-Azacytidine up regulates the expression of Epstein-Barr virus nuclear antigen 2 (EBNA-2) through EBNA-6 and latent membrane protein in the Burkitt's lymphoma line rael. J. Virol. 63, 3135-3141 (1989).
    • (1989) J. Virol. , vol.63 , pp. 3135-3141
    • Masucci, M.G.1
  • 22
    • 0031792779 scopus 로고    scopus 로고
    • Identification and characterization of a family of mammalian methyl-CpG binding proteins
    • Hendrich, B. & Bird, A.P. Identification and characterization of a family of mammalian methyl-CpG binding proteins. Mol. Cell. Biol. 18, 6538-6547 (1998).
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 6538-6547
    • Hendrich, B.1    Bird, A.P.2
  • 23
    • 0035542974 scopus 로고    scopus 로고
    • Methyl CpG-binding proteins and transcriptional repression
    • Wade, P. Methyl CpG-binding proteins and transcriptional repression. Bioessays 23, 1131-1137 (2001).
    • (2001) Bioessays , vol.23 , pp. 1131-1137
    • Wade, P.1
  • 24
    • 0037423186 scopus 로고    scopus 로고
    • The methyl-CpG-binding protein MeCP2 links DNA methylation to histone methylation
    • Fuks, F. et al. The methyl-CpG-binding protein MeCP2 links DNA methylation to histone methylation. J. Biol. Chem. 278, 4035-4040 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 4035-4040
    • Fuks, F.1
  • 25
    • 0022998473 scopus 로고
    • Trans-activation of a methylated adenovirus promoter by a frog virus 3 protein
    • Thompson, J.P., Granoff, A. & Willis, D.B. Trans-activation of a methylated adenovirus promoter by a frog virus 3 protein. Proc. Natl. Acad. Sci. USA 83, 7688-7692 (1986).
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 7688-7692
    • Thompson, J.P.1    Granoff, A.2    Willis, D.B.3
  • 27
    • 0033987840 scopus 로고    scopus 로고
    • Histone acetylation and reactivation of Epstein-Barr virus from latency
    • Jenkins, P.J., Binne, U.K. & Farrell, P.J. Histone acetylation and reactivation of Epstein-Barr virus from latency. J. Virol. 74, 710-720 (2000).
    • (2000) J. Virol. , vol.74 , pp. 710-720
    • Jenkins, P.J.1    Binne, U.K.2    Farrell, P.J.3
  • 28
    • 0038678667 scopus 로고    scopus 로고
    • Synergistic autoactivation of the Epstein-Barr virus immediate-early BRLF1 promoter by Rta and Zta
    • Liu, P. & Speck, S.H. Synergistic autoactivation of the Epstein-Barr virus immediate-early BRLF1 promoter by Rta and Zta. Virology 310, 199-206 (2003).
    • (2003) Virology , vol.310 , pp. 199-206
    • Liu, P.1    Speck, S.H.2
  • 29
    • 0032798394 scopus 로고    scopus 로고
    • The Epstein-Barr virus BZLF1 protein interacts physically and functionally with the histone acetylase CREB-binding protein
    • Adamson, A. & Kenney, S. The Epstein-Barr virus BZLF1 protein interacts physically and functionally with the histone acetylase CREB-binding protein. J. Virol. 73, 6551-6558 (1999).
    • (1999) J. Virol. , vol.73 , pp. 6551-6558
    • Adamson, A.1    Kenney, S.2
  • 30
    • 0037383691 scopus 로고    scopus 로고
    • The CBP bromodomain and nucleosome targeting are required for Zta-directed nucleosome acetylation and transcription activation
    • Deng, Z. et al. The CBP bromodomain and nucleosome targeting are required for Zta-directed nucleosome acetylation and transcription activation. Mol. Cell. Biol. 23, 2633-2644 (2003).
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 2633-2644
    • Deng, Z.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.