Silencing of the Epstein-Barr virus latent membrane protein 1 gene by the Max-Mad1-mSin3A modulator of chromatin structure

Journal of Virology

Volumn 73, Issue 4, 1999, Pages 2983-2993

  Sjöblom Hallén, Anna ^a   Yang, Weiwen ^a   Jansson, Ann ^a   Rymo, Lars ^a  

^a SAHLGRENSKA UNIVERSITY HOSPITAL   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

ACETIC ACID DERIVATIVE; CIS ACTING ELEMENT; HELIX LOOP HELIX PROTEIN; HISTONE DEACETYLASE; HISTONE H3; HISTONE H4; LATENT MEMBRANE PROTEIN 1; TRANSCRIPTION FACTOR;

ARTICLE; CELL TRANSFORMATION; CHROMATIN STRUCTURE; ENZYME ACTIVITY; ENZYME INHIBITION; EPSTEIN BARR VIRUS; GENE EXPRESSION REGULATION; GENE OVEREXPRESSION; GENE REPRESSION; GENE SILENCING; GENETIC TRANSCRIPTION; HUMAN; HUMAN CELL; NONHUMAN; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN BINDING; PROTEIN EXPRESSION; REGULATOR GENE; REPRESSOR GENE; SIGNAL TRANSDUCTION; TRANSACTIVATION; VIRUS ACTIVATION; VIRUS GENOME;

EID: 0033044134     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.73.4.2983-2993.1999     Document Type: Article

References (69)

1. Allday, M. J., D. H. Crawford, and J. A. Thomas. 1993. Epstein-Barr virus (EBV) nuclear antigen 6 induces expression of the EBV latent membrane protein and an activated phenotype in Raji cells. J. Gen. Virol. 74:361-369.
2. Amati, B., and H. Land. 1994. Myc-Max-Mad: a transcriplional factor network controlling cell cycle progression, differentiation and death. Curr. Biol. 4:102-108.
3. Atchley, W. R., and W. M. Fitch. 1997. A natural classification of the basic helix-loop-helix class of transcription factors. Proc. Natl. Acad. Sci. USA 94:5172-5176.
4. Ayer, D. E., L. Kretzner, and R. N. Eisenman. 1993. Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity. Cell 72:211-222.
5. Ayer, D. E., Q. A. Lawrence, and R. N. Eisenman. 1995. Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian nomologs of yeast repressor Sin3. Cell 80:767-776.
6. Bankier, A. T., P. L. Deininger, S. C. Satchwell, R. Baer, P. J. Farrell, and B. G. Barrell. 1983. DNA sequence analysis of the EcoRI Dhet fragment of B95-8 Epstein-Barr virus containing the terminal repeat sequences. Mol. Biol. Med. 1:425-445.
7. Ben-Bassat, H., N. Goldblum, S. Mitrani, T. Goldblum, J. M. Yoffey, M. M. Cohen, Z. Bentwich, B. Ramot, E. Klein, and G. Klein. 1977. Establishment in continuous culture of a new type of lymphocyte from a "Burkitt-like" malignant lymphoma (line D.G.-75). Int. J. Cancer 19:27-33.
8. Blackwell, T. K., J. Huang, A. Ma, L. Kretzner, F. W. Alt, R. N. Eisenman, and H. Weintraub. 1993. Binding of Myc proteins to canonical and noncanonical DNA sequences. Mol. Cell. Biol. 13:5216-5224.
9. Blackwell, T. K., and H. Weintraub. 1990. Differences and similarities in DNA-binding preferences of MyoD and E2A protein complexes revealed by binding site selection. Science 250:1104-1109.
10. Blackwood, E. M., and R. N. Eisenman. 1991. Max: a helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc. Science 251:1211-1217.
11. Blackwood, E. M., B. Luscher, and R. N. Eisenman. 1992. Myc and Max associate in vivo. Genes Dev. 6:71-80.
12. Boos, H., R. Berger, C. Kuklik-Roos, T. Iftner, and N. Mueller-Lantzsch. 1987. Enhancement of Epstein-Barr virus membrane protein (LMP) expression by serum, TPA, or n-butyrate in latently infected Raji cells. Virology 159:161-165.
13. Cohen, J. I., F. Wang, J. Mannick, and E. Kieff. 1989. Epstein-Barr virus nuclear protein 2 is a key determinant of lymphocyte transformation. Proc. Natl. Acad. Sci. USA 86:9558-9562.
14. Contreras-Salazar, B., B. Ehlin-Henriksson, G. Klein, and M. G. Masucci. 1990. Up regulation of the Epstein-Barr virus (EBV)-encoded membrane protein LMP in the Burkitt's lymphoma line Daudi after exposure to n-butyrate and after EBV superinfection. J. Virol. 64:5441-5447.
15. Dang, C. V., C. Dolde, M. L. Gillison, and G. J. Kato. 1992. Discrimination between related DNA sites by a single amino acid residue of Myc-related basic-helix-loop-helix proteins. Proc. Natl. Acad. Sci. USA 89:599-602.
16. Dyson, P., and P. J. Farrell. 1985. Chromatin structure of Epstein-Barr virus J. Gen. Virol. 66:1931-1940.
17. Ernberg, I., K. Falk, J. Minarovits, P. Busson, T. Tursz, M. G. Masucci, and G. Klein. 1989. 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.
18. Fåhraeus, R., A. Jansson, A. Ricksten, A. Sjöblom, and L. Rymo. 1990. Epstein-Barr virus-encoded nuclear antigen 2 activates the viral latent membrane protein promoter by modulating the activity of a negative regulatory element. Proc. Natl. Acad. Sci. USA 87:7390-7394.
19. Fåhraeus, R., A. Jansson, A. Sjöblom, T. Nilsson, G. Klein, and L. Rymo. 1993. Cell phenotype dependent control of Epstein-Barr virus latent membrane protein 1 (LMP1) gene regulatory sequences. Virology 195:71-80.
20. Fåhraeus, R., L. Palmqvist, A. Nerstedt, S. Farzad, L. Rymo, and S. Laín. 1994. Response to cAMP levels of the Epstein-Barr virus EBNA2-inducible LMP1 oncogene and EBNA2 inhibition of a PP1-like activity. EMBO J. 13:6041-6051.
21. Falk, K. I., L. Szekely, A. Aleman, and I. Ernberg. 1998. Specific methylation pattern in two control regions of Epstein-Barr virus latency: the LMP-1-coding upstream regulatory region and an origin of DNA replication (oriP). J. Virol. 72:2969-2974.
22. Farrell, P. J. 1998. Signal transduction from the Epstein-Barr virus LMP-1 transforming protein. Trends Microbiol. 6:175-177.
23. Fennewald, S., V. van Santen, and E. Kieff. 1984. Nucleotide sequence of an mRNA transcribed in latent growth-transforming virus infection indicates that it may encode a membrane protein. J. Virol. 51:411-419.
24. Gahn, T. A., and B. Sugden. 1995. An EBNA-1-dependent enhancer acts from a distance of 10 kilobase pairs to increase expression of the Epstein-Barr virus LMP gene. J. Virol. 69:2633-2636.
25. Hammerschmidt, W., and B. Sugden. 1989. Genetic analysis of immortalizing functions of Epstein-Barr virus in human B lymphocytes. Nature 340: 393-397.
26. Harada, S., and E. Kieff. 1997. Epstein-Barr virus nuclear protein LP stimulates EBNA-2 acidic domain-mediated transcriptional activation. J. Virol. 71:6611-6618.
27. Hinuma, Y., and J. T. Grace. 1967. Cloning of immunoglobulin-producing human leukemic and lymphoma cells in long-term cultures. Proc. Soc. Exp. Biol. Med. 124:107-111.
28. Hsieh, J. J.-D., and S. D. Hayward. 1995. Masking of the CBF1/RBPJκ transcriptional repression domain by Epstein-Barr virus EBNA2. Science 268:560-563.
29. Hurlin, P. J., C. Quéva, P. J. Koskinen, E. Steingrímsson, D. E. Ayer, N. G. Copeland, N. A. Jenkins, and R. N. Eisenman. 1995. Mad3 and Mad4: novel Max-interacting transcriptional repressors that suppress c-myc dependent transformation and are expressed during neural and epidermal differentiation. EMBO J. 14:5646-5659.
30. Johannsen, E., E. Koh, G. Mosialos, X. Tong, E. Kieff, and S. R. Grossman. 1995. Epstein-Barr virus nuclear protein 2 transactivation of the latent membrane protein 1 promoter is mediated by Jκ and PU.1. J. Virol. 69:253-262.
31. Kato, G. J., W. M. F. Lee, L. Chen, and C. V. Dang. 1992. Max: functional domains and interaction with c-Myc. Genes Dev. 6:81-92.
32. Kaye, K. M., K. M. Izumi, and E. Kieff. 1993. Epstein-Barr virus latent protein 1 is essential for B-lymphocyte growth transformation. Proc. Natl. Acad. Sci. USA 90:9150-9154.
33. Kieff, E. 1996. Epstein-Barr virus and its replication, p. 2343-2396. In B. N. Fields, D. M. Knipe, and P. M. Howley (ed.), Fields virology, 3rd ed. Lippincott-Raven Publishers, Philadelphia, Pa.
34. Klein, E.. G. Klein, J. S. Nadkarni, J. J. Nadkarni, H. Wigzell, and P. Clifford. 1968. Surface IgM-kappa specificity of a Burkitt lymphoma cell in vivo and in derived culture lines. Cancer Res. 28:1300-1310.
35. Klein, G., L. Dombos, and B. Gothoskar. 1972. Sensitivity of Epstein-Barr virus (EBV) producer and non-producer human lymphoblastoid cell lines to superinfection with EB-virus. Int. J. Cancer 10:44-57.
36. Laherty, C. D., W.-M. Yang, J.-M. Sun, J. R. Davie, E. Seto, and R. N. Eisenman. 1997. Histone deacetylases associated with the mSin3 corepressor mediate Mad transcriptional repression. Cell 89:349-356.
37. Laux, G., B. Adam, L. J. Strobl, and F. Moreau-Gachelin. 1994. The Spi-1/ PU.1 and Spi-B ets family transcription factors and the recombination signal binding protein RBP-Jκ interact with an Epstein-Barr virus nuclear antigen 2 responsive cis-element. EMBO J. 13:5624-5632.
38. Liebowitz, D., D. Wang, and E. Kieff. 1986. Orientation and patching of the latent infection membrane protein encoded by Epstein-Barr virus. J. Virol. 58:233-237.
39. Ling, P. D., D. R. Rawlins, and S. D. Hayward. 1993. The Epstein-Barr virus immortalizing protein EBNA-2 is targeted to DNA by a cellular enhancer-binding protein. Proc. Natl. Acad. Sci. USA 90:9237-9241.
40. Littlewood, T., and G. Evan. 1995. Transcription factors 2. Helix-loop-helix. Protein Profile 2:621-702.
41. Luka, J., B. Kallin, and G. Klein. 1979. Induction of the Epstein-Barr virus (EBV) cycle in latently infected cells by n-butyrate. Virology 94:228-231.
42. Mannick, J. B., J. I. Cohen, M. Birkenbach, A. Marchini, and E. Kieff. 1991. The Epstein-Barr virus nuclear protein encoded by the leader of the EBNA RNAs is important in B-lymphocyte transformation. J. Virol. 65:6826-6837.
43. Martin, J., and B. Sugden. 1991. The latent membrane protein oncoprotein resembles growth factor receptors in the properties of its turnover. Cell Growth Differ. 2:653-660.
44. Masucci, M. G., B. Contreras-Salazar, E. Ragnar, K. Falk, J. Minarovits, I. Ernberg, and G. Klein. 1989. 5-Azacytidine up-regulates the expression of Epstein-Barr virus nuclear antigen 2 (EBNA2) through EBNA-6 and latent membrane protein in the Burkitt's lymphoma line Rael. J. Virol. 63:3135-3141.
45. Minarovits, J., L.-F. Hu, S. Minarovits-Kormuta, G. Klein, and I. Ernberg. 1994. Sequence-specific methylation inhibits the activity of the Epstein-Barr virus LMP 1 and BCR2 enhancer-promoter regions. Virology 200:661-667.
46. Minarovits, J., S. Minarovits-Kormuta, B. Ehlin-Henriksson, K. Falk, G. Klein, and I. Ernberg. 1991. Host cell phenotype-dependent methylation patterns of Epstein-Barr virus DNA. J. Gen. Virol. 72:1591-1599.
47. Nan, X., H.-H. Ng, C. A. Johnson, C. D. Laherty, B. M. Turner, R. N. Eisenman, and A. Bird. 1998. Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves a histone deacetylase complex. Nature 393:386-389.
48. 2 repeat domain. J. Virol. 71:6619-6628.
49. Ohsako, S., J. Hyer, G. Panganiban, I. Oliver, and M. Caudy. 1994. Hairy function as a DNA-binding helix-loop-helix repressor of Drosophila sensory organ formation. Genes Dev. 8:2743-2755.
50. Pazin, M. J., and J. T. Kadonaga. 1997. What's up and down with histone deacetylation and transcription? Cell 89:325-328.
51. Rickinson, A. B., and E. Kieff. 1996. Epstein-Barr virus, p. 2397-2446. In B. N. Fields, D. M. Knipe, and P. M. Howley (ed.), Fields virology. 3rd ed. Lippincott-Raven Publishers. Philadelphia, Pa.
52. Ricksten, A., A. Olsson, T. Andersson, and L. Rymo. 1988. The 5′ flanking region of the gene for the Epstein-Barr virus-encoded nuclear antigen 2 contains a cell type specific cis-acting regulatory element that activates transcription in transfected B-cells. Nucleic Acids Res. 16:8391-8410.
53. Ricksten, A., C. Svensson, C. Welinder, and L. Rymo. 1987. Identification of sequences in Epstein-Barr virus DNA required for the expression of the second Epstein-Barr virus-determined nuclear antigen in COS-1 cells. J. Gen. Virol. 68:2407-2418.
54. Rowe, M., H. S. Evans, L. S. Young, K. Hennessy, E. Kieff, and A. B. Rickinson. 1987. Monoclonal antibodies to the latent membrane protein of Epstein-Barr virus reveal heterogeneity of the protein and inducible expression in virus-transformed cells. J. Gen. Virol. 68:1575-1586.
55. Rowe, M., A. L. Lear, D. Croom-Carter, A. H. Davies, and A. B. Rickinson. 1992. Three pathways of Epstein-Barr virus gene activation from EBNA1-positive latency in B lymphocytes. J. Virol. 66:122-131.
56. Shaw, J. E., L. F. Levinger, and C. W. Carter. 1979. Nucleosomal structure of Epstein-Barr virus DNA in transformed cell lines. J. Virol. 29:657-665.
57. Shikama, N., J. Lyon, and N. B. La Thangue. 1997. The p300/CBP family: integrating signals with transcription factors and chromatin. Trends Cell Biol. 7:230-236.
58. Sjöblom, A., A. Jansson, W. Yang, S. Laín, T. Nilsson, and L. Rymo. 1995. PU box-binding transcription factors and a POU domain protein cooperate in the Epstein-Barr virus (EBV) nuclear antigen 2-induced transactivation of the EBV latent membrane protein 1 promoter. J. Gen. Virol. 76:2679-2692.
59. Sjöblom, A., A. Nerstedt, A. Jansson, and L. Rymo. 1995. Domains of the Epstein-Barr virus nuclear antigen 2 (EBNA2) involved in the transactivation of the latent membrane protein 1 and the EBNA Cp promoters. J. Gen. Virol. 76:2669-2678.
60. Sjöblom, A., W. Yang, L. Palmqvist, A. Jansson, and L. Rymo. 1998. An ATF/CRE element mediates both EBNA2-dependent and EBNA2-independent activation of the Epstein-Barr virus LMP1 gene promoter. J. Virol. 72:1365-1376.
61. Solomon, D. L. C., B. Amati, and H. Land. 1993. Distinct DNA binding preferences for the c-Myc/Max and Max/Max dimers. Nucleic Acids Res. 21:5372-5376.
62. Tomkinson, B., E. Robertson, and E. Kieff. 1993. Epstein-Barr virus nuclear proteins EBNA-3A and EBNA-3C are essential for B-lymphocyte growth transformation. J. Virol. 67:2014-2025.
63. Viollet, B., A.-M. Lefrançois-Martinez, A. Henrion, A. Kahn, M. Raymondjean, and A. Martinez. 1996. Immunochemical characterization and transacting properties of upstream stimulatory factor isoforms. J. Biol. Chem. 271:1405-1415.
64. Waltzer, L., P. Y. Bourillot, A. Sergeant, and E. Manet. 1995. RBP-Jκ repression activity is mediated by a co-repressor and antagonized by the Epstein-Barr virus transcription factor EBNA2. Nucleic Acids Res. 23:4939-4945.
65. Wu, D. Y., G. V. Kalpana, S. P. Goff, and W. H. Schubach. 1996. Epstein-Barr virus nuclear protein 2 (EBNA2) binds to a component of the human SNF-SWI complex, hSNF5/Ini1. J. Virol. 70:6020-6028.
66. Yalamanchili, R., X. Tong, S. Grossman, J. E., G. Mosialos, and E. Kieff. 1994. Genetic and biochemical evidence that EBNA2 interaction with a 63-kDa cellular GTG-binding protein is essential for B lymphocyte growth transformation by EBV. Virology 204:634-641.
67. Yates, J. L., N. Warren, and B. Sugden. 1985. Stable replication of plasmids derived from Epstein-Barr virus in a variety of mammalian cells. Nature 313:812-815.
68. Zervos, A. S., J. Gyuris, and R. Brent. 1993. Mxi1, a protein that specifically interacts with Max to bind Myc-Max recognition sites. Cell 72:223-232.
69. κ, the homologue of Drosophila Suppressor of Hairless. EMBO J. 13:4973-4982.