A conserved domain of the Epstein-Barr virus nuclear antigens 3A and 3C binds to a discrete domain of Jκ

Journal of Virology

Volumn 70, Issue 7, 1996, Pages 4228-4236

  Zhao, B O ^a   Marshall, Dana R ^b   Sample, Clare E ^a,b  

^a UNIVERSITY OF TENNESSEE COLLEGE OF MEDICINE   (United States)

^b ST JUDE CHILDREN S RESEARCH HOSPITAL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; NUCLEAR PROTEIN; VIRUS ANTIGEN;

ARTICLE; B LYMPHOCYTE; CONTROLLED STUDY; DNA SEQUENCE; DROSOPHILA; EPSTEIN BARR VIRUS; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN DOMAIN; TRANSACTIVATION; VIRUS CELL TRANSFORMATION; VIRUS TRANSCRIPTION;

EID: 0029974216     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.70.7.4228-4236.1996     Document Type: Article

References (49)

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. 1-arrested cells. J. Virol. 68:3491-3498.
3. Amakawa, R., W. Jing, K. Ozawa, N. Matsunami, V. Hamaguchi, F. Matsuda, M. Kawaichi, and T. Honjo. 1993. Human Jκ recombination signal binding protein gene (IGKJRB): comparison with its mouse homologue. Genomics 17:306-315.
4. Baichwal, V. R., and B. Sugden. 1988. Transformation of Balb 3T3 cells by the BNLF-1 gene of Epstein-Barr virus. Oncogene 2:463-467.
5. Bang, A. G., and J. W. Posakony. 1992. The Drosophila gene Hairless encodes a novel basic protein that controls alternative cell fates in adult sensory organ development. Genes Dev. 6:1752-1769. (Erratum, 6:2233.)
6. Bodescot, M., O. Brison, and M. Perricaudet. 1986. An Epstein-Barr virus transcription unit is at least 84 kilobases long. Nucleic Acids Res. 14:2611-2620.
7. Bohnsack, J. F., and N. R. Cooper. 1988. CR2 ligands modulate human B cell activation. J. Immunol. 141:2569-2576.
8. Bonnefoy, J. Y., S. Henchoz, D. Hardie, M. J. Holder, and J. Gordon. 1993. A subset of anti-CD21 antibodies promote the rescue of germinal center B cells from apoptosis. Eur. J. Immunol. 23:969-972.
9. Bram, R. J., and G. R. Crabtree. 1994. Calcium signalling in T cells stimulated by a cyclophilin B-binding protein. Nature (London) 371:355-358.
10. Brou, C., F. Logeat, M. Lecourtois, J. Vandekerckhove, P. Kourilsky, F. Schweisguth, and A. Israel. 1994. Inhibition of the DNA-binding activity of Drosophila suppressor of hairless and of its human homolog, KBF2/RBP-J kappa, by direct protein-protein interaction with Drosophila hairless. Genes Dev. 8:2491-2503.
11. Busch, S. J., and P. Sassone-Corsi. 1990. Dimers. leucine zippers and DNA-binding domains. Trends Genet, 6:36-40.
12. Chung, C. N., Y. Hamaguchi, T. Honjo, and M. Kawaichi. 1994. Site-directed mutagenesis study on DNA binding regions of the mouse homologue of Suppressor of Hairless, RBP-J kappa. Nucleic Acids Res. 22:2938-2944.
13. Don, S., X. Zeng, P. Cortes, H. Erdjument-Bromage, P. Tempst, T. Honjo, and L. D. Vales. 1994. The recombination signal sequence-binding protein RBP-2N functions as a transcriptional repressor. Mol. Cell. Biol. 14:3310-3319.
14. Durfee, T., K. Becherer, P. L. Chen, S. H. Yeh, Y. Yang, A. E. Kilburn, W. H. Lee, and S. J. Elledge. 1993. The retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunit. Genes Dev. 7:555-569.
15. Fields, S., and O. Song. 1989. A novel genetic system to detect protein-protein interactions. Nature (London) 340:245-246.
16. Frade, R., J. Hermann, and M. Barel. 1992. A 16 amino acid synthetic peptide derived from human C3d triggers proliferation and specific tyrosine phosphorylation of transformed CR2-positive human lymphocytes and of normal resting B lymphocytes. Biochem. Biophys. Res. Commun. 188:833-842.
17. Funikawa, T., S. Maruyama, M. Kawaichi, and T. Honjo. 1992. The Drosophila homolog of the immunoglobulin recombination signal-binding protein regulates peripheral nervous system development. Cell 69:1191-1197.
18. Grossman, S. R., E. Johannsen, X. Tong, R. Yalamanchili, and E. Kieff. 1994. The Epstein-Barr virus nuclear antigen 2 transactivator is directed to response elements by the Jκ recombination signal binding protein. Proc. Natl. Acad. Sci. USA 91:7568-7572.
19. Hammerschmidt, W., B. Sugden, and V. R. Baichwal. 1989. The transforming domain alone of the latent membrane protein of Epstein-Barr virus is toxic to cells when expressed at high levels. J. Virol. 63:2469-2475.
20. Harper, J. W., G. R. Adami, N. Wei, K. Keyomarsi, and S. J. Elledge. 1993. The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases. Cell 75:805-816.
21. Henkel, T., P. D. Ling, S. D. Hayward, and M. G. Peterson. 1994. Mediation of Epstein-Barr virus EBNA2 transactivation by recombination signal-binding protein J kappa. Science 265:92-95.
22. Hsieh, J. J., and S. D. Hayward. 1995. Masking of the CBF1/RBPJ kappa transcriptional repression domain by Epstein-Barr virus EBNA2. Science 268:560-563.
23. Ito, H., Y. Fukuda, K. Murata, and A. Kimura. 1983. Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153:163-168.
24. Joab, I., D. T. Rowe, M. Bodescot, J. C. Nicolas, P. J. Farrell, and M. Perricaudet. 1987. Mapping of the gene coding for Epstein-Barr virus-determined nuclear antigen EBNA3 and its transient overexpression in a human cell line by using an adenovirus expression vector. J. Virol. 61:3340-3344.
25. 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.l. J. Virol. 69:253-262.
26. Kawaichi, M., C. Oka, S. Shibayama, A. E. Koromilas, N. Matsunami, Y. Hamaguchi, and T. Honjo. 1992. Genomic organization of mouse J kappa recombination signal binding protein (RBP-J kappa) gene. J. Biol. Chem. 267:4016-4022.
27. Kerdiles, B., D. Walls, H. Triki, M. Perricaudet, and I. Joab. 1990. cDNA cloning and transient expression of the Epstein-Barr virus-determined nuclear antigen EBNA3B in human cells and identification of novel transcripts from its coding region. J. Virol. 64:1812-1816.
28. Kieff, E., and D. Liebowitz. 1990. Epstein-Barr virus and its replication, p. 1889-1920. In B. Fields, D. Knipe, R. Chanock, M. Hirsch, J. Melnick, T. Monath, and B. Roizman (ed.), Virology. Raven Press Ltd., New York.
29. Landschultz, W. H., P. F. Johnson, and S. L. McKnight. 1988. The leucine zipper: a hypothetical structure common to a new class of DNA binding proteins. Science 240:1759-1764.
30. Le Roux, A., B. Kerdiles, D. Walls, J. F. Dedieu, and M. Perricaudet. 1994. The Epstein-Barr virus determined nuclear antigens EBNA-3A, -3B, and -3C repress EBNA-2-mediated transactivation of the viral terminal protein 1 gene promoter. Virology 205:596-602.
31. 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.
32. Marshall, D., and C. Sample. 1995. Epstein-Barr virus nuclear antigen 3C is a transcriptional regulator. J. Virol, 69:3624-3630.
33. 32a.Maunders, M. J., L. Petti, and M. Rowe. 1994. Precipitation of the Epstein-Barr virus protein EBNA 2 by an EBNA 3c-specific monoclonal antibody. J. Gen. Virol. 75:769-778.
34. Meitinger, C., L. J. Strobl, G. Marschall, G. W. Bornkamm, and U. Zimber-Strobl. 1994. Crucial sequences within the Epstein-Barr virus TP1 promoter for EBNA2-mediated transactivation and interaction of EBNA2 with its responsive element. J. Virol. 68:7497-7506.
35. Miller, G. 1985. Epstein-Barr virus: biology, pathogenesis, and medical aspects, p. 1921-1958. In B. N. Fields, D. M. Knipe, R. M. Chanock, J. L. Melnick, B. Roizman, and R. E. Shope (ed.), Virology. Raven Press, New York.
36. Miller, J. H. 1972. Experiments in molecular genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
37. Nemerow, G. R., M. E. McNaughton, and N. R. Cooper. 1985. Binding of monoclonal antibody to the Epstein Barr virus (EBV)/CR2 receptor induces activation and differentiation of human B lymphocytes. J. Immunul. 135:3068-3073.
38. Petti, L., and E. Kieff. 1988. A sixth Epstein-Barr virus nuclear protein (EBNA3B) is expressed in latently infected growth-transformed lymphocytes. J. Virol. 62:2173-2178.
39. Petti, L., J. Sample, F. Wang, and E. Kieff. 1988. A fifth Epstein-Barr virus nuclear protein (EBNA3C) is expressed in latently infected growth-transformed lymphocytes. J. Virol. 62:1330-1338.
40. Ricksten, A., B. Kallin, H. Alexander, J. Dillner, R. Fahraeus, G. Klein, R. Lerner, and L. Rymo. 1988. BamHI E region of the Epstein-Barr virus genome encodes three transformation-associated nuclear proteins. Proc. Natl. Acad. Sci. USA 85:995-999.
41. Robertson, E. S., S. Grossman, E. Johannsen, C. Miller, J. Lin, B, Tonikinson, and E. Kieff. 1995. Epstein-Barr virus nuclear protein 3C modulates transcription through interaction with the sequence-specific DNA-hinding protein Jκ. J. Virol. 69:3108-3116.
42. Sample, C. E., and B. D. Parker. 1994. Biochemical characterization of the Epstein-Barr virus nuclear antigen 3A and 3C proteins. Virology 205:535-539.
43. Sample, J., E. B. Henson, and C. Sample. 1992. The Epstein-Barr virus nuclear protein 1 promoter active in type I latency is autoregulated. J. Virol. 66:4654-4661.
44. Smith, D. B., and K. S. Johnson. 1988. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene 67:31-40.
45. Tomkinson, B., and E. Kieff. 1992. Use of second-site homologous recombination to demonstrate that Epstein-Barr virus nuclear protein 3B is not important for lymphocyte infection or growth transformation in vitro. J. Virol. 66:2893-2903.
46. 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.
47. Wang, D., D. Liebowitz, and E. Kieff. 1985. An EBV membrane protein expressed in immortalized lymphocytes transforms established rodent cells. Cell 43:831-840.
48. Wang, F., C. Gregory, C. Sample, M. Rowe, D. Liebowitz, R. Murray, A. Rickinson, and E. Kieff. 1990. Epstein-Barr virus latent membrane protein (LMP1) and nuclear proteins 2 and 3C are effectors of phenotypic changes in B lymphocytes: EBNA-2 and LMP1 cooperatively induce CD23. J. Virol. 64:2309-2318.
49. Zimber-Strobl, U., L. J. Strobl, C. Meitinger, K. Hinrichs, T. Sakai, T. Furukawa, T. Honjo, and G. W. Bornkamm. 1994. Epstein-Barr virus nuclear antigen 2 exerts its transactivating function through interaction with recombination signal binding protein RBP-J kappa, the homologue of Drosophila Suppressor of Hairless. EMBO J. 13:4973-4982.