Modulation of Histone Acetyltransferase Activity through Interaction of Epstein-Barr Nuclear Antigen 3C with Prothymosin Alpha

REFERENCES

• Aiyar, A., Tyree, C., and Sugden, B.. 1998. The plasmid replicon of EBV consists of multiple cis-acting elements that facilitate DNA synthesis by the cell and a viral maintenance element. EMBO J. 17:6394–6403
   PubMed Web of Science ®Google Scholar
• Alfieri, C., Birkenbach, M., and Kieff, E.. 1991. Early events in Epstein-Barr virus infection of human B lymphocytes. Virology 181:595–608 (Erratum, 185:946.)
   PubMed Web of Science ®Google Scholar
• Ambinder, R. F.. 1990. Human lymphotropic viruses associated with lymphoid malignancy: Epstein-Barr and HTLV-1. Hematol. Oncol. Clin. N. Am. 4:821–833
   PubMed Web of Science ®Google Scholar
• Artavanis-Tsakonas, S., Matsuno, K., and Fortini, M. E.. 1995. Notch signaling. Science 268:225–232
   PubMed Web of Science ®Google Scholar
• Artavanis-Tsakonas, S., Rand, M. D., and Lake, R. J.. 1999. Notch signaling: cell fate control and signal integration in development. Science 284:770–776
   PubMed Web of Science ®Google Scholar
• Aster, J. C., Robertson, E. S., Hasserjian, R. P., Turner, J. R., Kieff, E., and Sklar, J.. 1997. Oncogenic forms of NOTCH1 lacking either the primary binding site for RBP-Jκ or nuclear localization sequences retain the ability to associate with RBP-Jκ and activate transcription. J. Biol. Chem. 272:11336–11343
   PubMedGoogle Scholar
• Bain, M., Watson, R. J., Farrell, P. J., and Allday, M. J.. 1996. Epstein-Barr virus nuclear antigen 3C is a powerful repressor of transcription when tethered to DNA. J. Virol. 70:2481–2489
   PubMedGoogle Scholar
• Brou, C., Logeat, F., Lecourtois, M., Vandekerckhove, J., Kourilsky, P., Schweisguth, F., and Israel, A.. 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
   PubMed Web of Science ®Google Scholar
• Chakravarti, D., LaMorte, V. J., Nelson, M. C., Nakajima, T., Schulman, I. G., Juguilon, H., Montminy, M., and Evans, R. M.. 1996. Role of CBP/P300 in nuclear receptor signalling. Nature 383:99–103
   PubMed Web of Science ®Google Scholar
• Chakravarti, D., Ogryzko, V., Kao, H. Y., Nash, A., Chen, H., Nakatani, Y., and Evans, R. M.. 1999. A viral mechanism for inhibition of p300 and PCAF acetyltransferase activity. Cell 96:393–403
   PubMed Web of Science ®Google Scholar
• Cohen, J. I., Wang, F., Mannick, J., and Kieff, E.. 1989. Epstein-Barr virus nuclear protein 2 is a key determinant of lymphocyte transformation. Proc. Natl. Acad. Sci. USA 86:9558–9562
   PubMed Web of Science ®Google Scholar
• Diaz-Jullien, C., Perez-Estevez, A., Covelo, G., and Freire, M.. 1996. Prothymosin alpha binds histones in vitro and shows activity in nucleosome assembly assay. Biochim. Biophys. Acta 1296:219–227
   PubMedGoogle Scholar
• Dominguez, F., Magdalena, C., Cancio, E., Roson, E., Paredes, J., Loidi, L., Zalvide, J., Fraga, M., Forteza, J., Regueiro, B. J. et al. 1993. Tissue concentrations of prothymosin alpha: a novel proliferation index of primary breast cancer. Eur. J. Cancer 6:893–897
   Google Scholar
• Eckner, R., Ewen, M. E., Newsome, D., Gerdes, M., DeCaprio, J. A., Lawrence, J. B., and Livingston, D. M.. 1994. Molecular cloning and functional analysis of the adenovirus E1A-associated 300-kD protein (p300) reveals a protein with properties of a transcriptional adaptor. Genes Dev. 8:869–884
   PubMed Web of Science ®Google Scholar
• Eilers, M., Schirm, S., and Bishop, J. M.. 1991. The MYC protein activates transcription of the alpha-prothymosin gene. EMBO J. 10:133–141
   PubMed Web of Science ®Google Scholar
• Eschenfeldt, W. H., and Berger, S. L.. 1986. The human prothymosin alpha gene is polymorphic and induced upon growth stimulation: evidence using a cloned cDNA. Proc. Natl. Acad. Sci. USA 83:9403–9407
   PubMed Web of Science ®Google Scholar
• Felzien, L. K., Farrell, S., Betts, J. C., Mosavin, R., and Nabel, G. J.. 1999. Specificity of cyclin E-Cdk2, TFIIB, and E1A interactions with a common domain of the p300 coactivator. Mol. Cell. Biol. 19:4241–4246
   PubMedGoogle Scholar
• Felzien, L. K., Woffendin, C., Hottiger, M. O., Subbramanian, R. A., Cohen, E. A., and Nabel, G. J.. 1998. HIV transcriptional activation by the accessory protein, VPR, is mediated by the p300 co-activator. Proc. Natl. Acad. Sci. USA 95:5281–5286
   PubMed Web of Science ®Google Scholar
• Frangou-Lazaridis, M., Clinton, M., Goodall, G. J., and Horecker, B. L.. 1988. Prothymosin alpha and parathymosin: amino acid sequences deduced from the cloned rat spleen cDNAs. Arch. Biochem. Biophys. 263:305–310
   PubMedGoogle Scholar
• Gahn, T. A., and Sugden, B.. 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
   PubMedGoogle Scholar
• Gast, K., Damaschun, H., Eckert, K., Schulze-Forster, K., Maurer, H. R., Muller-Frohne, M., Zirwer, D., Czarnecki, J., and Damaschun, G.. 1995. Prothymosin alpha: a biologically active protein with random coil conformation. Biochemistry 34:13211–13218
   PubMed Web of Science ®Google Scholar
• Giles, R. H., Peters, D. J. M., and Breuning, M. H.. 1998. Conjunction dysfunction: CBP/p300 in human disease. Trends Genet. 14:178–183
   PubMed Web of Science ®Google Scholar
• Gomez-Marquez, J., and Rodriguez, P.. 1998. Prothymosin alpha is a chromatin-remodelling protein in mammalian cells. Biochem. J. 333:1–3
   PubMedGoogle Scholar
• Gomez-Marquez, J., and Segade, F.. 1988. Prothymosin alpha is a nuclear protein. FEBS Lett. 226:217–219
   PubMed Web of Science ®Google Scholar
• Gomez-Marquez, J., Segade, F., Dosil, M., Pichel, J. G., Bustelo, X. R., and Freire, M.. 1989. The expression of prothymosin alpha gene in T lymphocytes and leukemic lymphoid cells is tied to lymphocyte proliferation. J. Biol. Chem. 264:8451–8454
   PubMed Web of Science ®Google Scholar
• Goodall, G. J., Dominguez, F., and Horecker, B. L.. 1986. Molecular cloning of cDNA for human prothymosin alpha. Proc. Natl. Acad. Sci. USA 83:8926–8928
   PubMed Web of Science ®Google Scholar
• Graziano, V., Gerchman, S. E., Schneider, D. K., and Ramakrishnan, V.. 1994. Histone H1 is located in the interior of the chromatin 30-nm filament. Nature 368:351–354
   PubMedGoogle Scholar
• Hamamori, Y., Sartorelli, V., Ogryzko, V., Puri, P. L., Wu, H. Y., Wang, J. Y., Nakatani, Y., and Kedes, L.. 1999. Regulation of histone acetyltransferases p300 and PCAF by the bHLH protein twist and adenoviral oncoprotein E1A. Cell 96:405–413
   PubMed Web of Science ®Google Scholar
• Hammerschmidt, W., and Sugden, B.. 1989. Genetic analysis of immortalizing functions of Epstein-Barr virus in human B lymphocytes. Nature 340:393–397
   PubMed Web of Science ®Google Scholar
• Harper, J. W., Adami, G. R., Wei, N., Keyomarsi, K., and Elledge, S. J.. 1993. The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases. Cell 75:805–816
   PubMed Web of Science ®Google Scholar
• Harper, J. W., Elledge, S. J., Keyomarsi, K., Dynlacht, B., Tsai, L. H., Zhang, P., Dobrowolski, S., Bai, C., Connell-Crowley, L., Swindell, E. et al. 1995. Inhibition of cyclin-dependent kinases by p21. Mol. Biol. Cell 6:387–400
   PubMed Web of Science ®Google Scholar
• Hartzog, G. A., and Winston, F.. 1997. Nucleosomes and transcription: recent lessons from genetics. Curr. Opin. Genet. Dev. 7:192–198
   PubMedGoogle Scholar
• Hitt, M. M., Allday, M. J., Hara, T., Karran, L., Jones, M. D., Busson, P., Tursz, T., Ernberg, I., and Griffin, B. E.. 1989. EBV gene expression in an NPC-related tumour. EMBO J. 8:2639–2651
   PubMed Web of Science ®Google Scholar
• Hsieh, J. J., Henkel, T., Salmon, P., Robey, E., Peterson, M. G., and Hayward, S. D.. 1996. Truncated mammalian Notch1 activates CBF1/RBPJk-repressed genes by a mechanism resembling that of Epstein-Barr virus EBNA2. Mol. Cell. Biol. 16:952–959
   PubMedGoogle Scholar
• Imhof, A., Yang, X. J., Ogryzko, V. V., Nakatani, Y., Wolffe, A. P., and Ge, H.. 1997. Acetylation of general transcription factors by histone acetyltransferases. Curr. Biol. 7:689–692
   PubMed Web of Science ®Google Scholar
• Johannsen, E., Miller, C. L., Grossman, S. R., and Kieff, E.. 1996. EBNA-2 and EBNA-3C extensively and mutually exclusively associate with RBPJκ in Epstein-Barr virus-transformed B lymphocytes. J. Virol. 70:4179–4183
   PubMedGoogle Scholar
• Kamei, Y., Xu, L., Heinzel, T., Torchia, J., Kurokawa, R., Gloss, B., Lin, S. C., Heyman, R. A., Rose, D. W., Glass, C. K., and Rosenfeld, M. G.. 1996. A CBP integrator complex mediates transcriptional activation and AP-1 inhibition by nuclear receptors. Cell 85:403–414
   PubMed Web of Science ®Google Scholar
• Kao, H. Y., Ordentlich, P., Koyano-Nakagawa, N., Tang, Z., Downes, M., Kintner, C. R., Evans, R. M., and Kadesch, T.. 1998. A histone deacetylase corepressor complex regulates the Notch signal transduction pathway. Genes Dev. 12:2269–2277
   PubMed Web of Science ®Google Scholar
• Karetsou, Z., Sandaltzopoulos, R., Frangou-Lazaridis, M., Lai, C. Y., Tsolas, O., Becker, P. B., and Papamarcaki, T.. 1998. Prothymosin alpha modulates the interaction of histone H1 with chromatin. Nucleic Acids Res. 26:3111–3118
   PubMed Web of Science ®Google Scholar
• Kaye, K. M., Izumi, K. M., and Kieff, E.. 1993. Epstein-Barr virus latent membrane protein 1 is essential for B-lymphocyte growth transformation. Proc. Natl. Acad. Sci. USA 90:9150–9154
   PubMed Web of Science ®Google Scholar
• Kieff, E.. Epstein-Barr virus and its replication, 3rd ed. 2: Lippincott-Raven, Philadelphia, Pa
   Google Scholar
• Kirchmaier, A. L., and Sugden, B.. 1997. 1996. Dominant-negative inhibitors of EBNA-1 of Epstein-Barr virus. J. Virol. 71:1766–1775
   PubMedGoogle Scholar
• Kouzarides, T.. 1999. Histone acetylases and deacetylases in cell proliferation. Curr. Opin. Genet. Dev. 9:40–48
   PubMed Web of Science ®Google Scholar
• Le Roux, A., Kerdiles, B., Walls, D., Dedieu, J. F., and Perricaudet, M.. 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
   PubMedGoogle Scholar
• Ling, P. D., Rawlins, D. R., and Hayward, S. D.. 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
   PubMedGoogle Scholar
• Loidi, L., Vidal, A., Zalvide, J. B., Puente, J. L., Reyes, F., and Dominguez, F.. 1997. Development of ELISA to estimate thymosin alpha1, the N terminus of prothymosin alpha, in human tumors. Clin. Chem. 43:59–63
   PubMed Web of Science ®Google Scholar
• Longnecker, R.. 1994. Biochemical and genetic studies of Epstein-Barr virus latent membrane protein 2. Leukemia 8 (Suppl. 1):S46–S50
   PubMed Web of Science ®Google Scholar
• Lundblad, J. R., Kwok, R. P., Laurance, M. E., Harter, M. L., and Goodman, R. H.. 1995. Adenoviral E1A-associated protein p300 as a functional homologue of the transcriptional co-activator CBP. Nature 374:85–88
   PubMed Web of Science ®Google Scholar
• Mannick, J. B., Cohen, J. I., Birkenbach, M., Marchini, A., and Kieff, E.. 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
   PubMedGoogle Scholar
• Manrow, R. E., and Berger, S. L.. 1993. GAG triplets as splice acceptors of last resort. An unusual form of alternative splicing in prothymosin alpha pre-mRNA. J. Mol. Biol. 234:281–288
   PubMed Web of Science ®Google Scholar
• Manrow, R. E., Sburlati, A. R., Hanover, J. A., and Berger, S. L.. 1991. Nuclear targeting of prothymosin alpha. J. Biol. Chem. 266:3916–3924
   PubMed Web of Science ®Google Scholar
• Marchini, A., Longnecker, R., and Kieff, E.. 1992. Epstein-Barr virus (EBV)-negative B-lymphoma cell lines for clonal isolation and replication of EBV recombinants. J. Virol. 66:4972–4981
   PubMedGoogle Scholar
• Marshall, D., and Sample, C.. 1995. Epstein-Barr virus nuclear antigen 3C is a transcriptional regulator. J. Virol. 69:3624–3630
   PubMedGoogle Scholar
• Maunders, M. J., Petti, L., and Rowe, M.. 1994. Precipitation of the Epstein-Barr virus protein EBNA 2 by an EBNA 3c-specific monoclonal antibody. J. Gen. Virol. 75:769–787
   PubMedGoogle Scholar
• Moran, E.. 1993. DNA tumor virus transforming proteins and the cell cycle. Curr. Opin. Genet. Dev. 3:63–70
   PubMed Web of Science ®Google Scholar
• Mori, M., Barnard, G. F., Staniunas, R. J., Jessup, J. M., Steele, G. D.Jr., and Chen, L. B.. 1993. Prothymosin-alpha mRNA expression correlates with that of c-myc in human colon cancer. Oncogene 8:2821–2826
   PubMed Web of Science ®Google Scholar
• Mosialos, G., Birkenbach, M., Yalamanchili, R., VanArsdale, T., Ware, C., and Kieff, E.. 1995. The Epstein-Barr virus transforming protein LMP1 engages signaling proteins for the tumor necrosis factor receptor family. Cell 80:389–399
   PubMed Web of Science ®Google Scholar
• Ogryzko, V. V., Schiltz, R. L., Russanova, V., Howard, B. H., and Nakatani, Y.. 1996. The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell 87:953–959
   PubMed Web of Science ®Google Scholar
• Perkins, N. D., Felzien, L. K., Betts, J. C., Leung, K., Beach, D. H., and Nabel, G. J.. 1997. Regulation of NF-κB by cyclin-dependent kinases associated with the p300 coactivator. Science 275:523–527
   PubMed Web of Science ®Google Scholar
• Puri, P. L., Sartorelli, V., Yang, X. J., Hamamori, Y., Ogryzko, V. V., Howard, B. H., Kedes, L., Wang, J. Y., Graessmann, A., Nakatani, Y., and Levrero, M.. 1997. Differential roles of p300 and PCAF acetyltransferases in muscle differentiation. Mol. Cell 1:35–45
   PubMed Web of Science ®Google Scholar
• Raab-Traub, N., and Webster-Cyriaque, J.. 1997. Epstein-Barr virus infection and expression in oral lesions. Oral Dis. 3 (Suppl. 1):S164–S170
   PubMedGoogle Scholar
• Radkov, S. A., Touitou, R., Brehm, A., Rowe, M., West, M., Kouzarides, T., and Allday, M. J.. 1999. Epstein-Barr virus nuclear antigen 3C interacts with histone deacetylase to repress transcription. J. Virol. 73:5688–5697
   PubMed Web of Science ®Google Scholar
• Rickinson, A., and E. K. 1996. Epstein-Barr virus, 3rd ed., vol. 2. Lippincott-Raven, Philadelphia, Pa.
   Google Scholar
• Robertson, E. S.. 1997. The Epstein-Barr virus EBNA3 protein family as regulators of transcription. Epstein-Barr Virus Rep. 4:143–150
   Google Scholar
• Robertson, E. S., and Kieff, E.. 1995. Genetic analysis of Epstein-Barr virus in B lymphocytes. Epstein-Barr Virus Rep. 2:73–80
   Google Scholar
• Robertson, E. S., Grossman, S., Johannsen, E., Miller, C., Lin, J., Tomkinson, B., and Kieff, E.. 1995. Epstein-Barr virus nuclear protein 3C modulates transcription through interaction with the sequence-specific DNA-binding protein Jκ. J. Virol. 69:3108–3116
   PubMedGoogle Scholar
• Robertson, E. S., Lin, J., and Kieff, E.. 1996. The amino-terminal domains of Epstein-Barr virus nuclear proteins 3A, 3B, and 3C interact with RBPJκ. J. Virol. 70:3068–3074
   PubMed Web of Science ®Google Scholar
• Rodriguez, P., Vinuela, J. E., Alvarez-Fernandez, L., Buceta, M., Vidal, A., Dominguez, F., and Gomez-Marquez, J.. 1998. Overexpression of prothymosin alpha accelerates proliferation and retards differentiation in HL-60 cells. Biochem. J. 331:753–761
   PubMedGoogle Scholar
• Sample, J., Young, L., Martin, B., Chatman, T., Kieff, E., and Rickinson, A.. 1990. Epstein-Barr virus types 1 and 2 differ in their EBNA-3A, EBNA-3B, and EBNA-3C genes. J. Virol. 64:4084–4092
   PubMed Web of Science ®Google Scholar
• Sburlati, A. R., Manrow, R. E., and Berger, S. L.. 1990. Human prothymosin alpha: purification of a highly acidic nuclear protein by means of a phenol extraction. Protein Expr. Purif. 1:184–190
   PubMedGoogle Scholar
• Sburlati, A. R., Manrow, R. E., and Berger, S. L.. 1991. Prothymosin alpha antisense oligomers inhibit myeloma cell division. Proc. Natl. Acad. Sci. USA 88:253–257
   PubMed Web of Science ®Google Scholar
• Shikama, N., Lyon, J., and LaThangue, N.. 1997. The p300/CBP family: integrating signals with transcription factors and chromatin. Trends Cell Biol. 7:230–235
   PubMedGoogle Scholar
• Sixbey, J. W., Nedrud, J. G., Raab-Traub, N., Hanes, R. A., and Pagano, J. S.. 1984. Epstein-Barr virus replication in oropharyngeal epithelial cells. N. Engl. J. Med. 310:1225–1230
   PubMed Web of Science ®Google Scholar
• Sternglanz, R.. 1996. Histone acetylation: a gateway to transcriptional activation. Trends Biochem. Sci. 21:357–358
   PubMedGoogle Scholar
• Struhl, K.. 1998. Histone acetylation and transcription regulatory mechanisms. Genes Dev. 12:599–606
   PubMed Web of Science ®Google Scholar
• Swaminathan, S., Tomkinson, B., and Kieff, E.. 1991. Recombinant Epstein-Barr virus with small RNA (EBER) genes deleted transforms lymphocytes and replicates in vitro. Proc. Natl. Acad. Sci. USA 88:1546–1550
   PubMed Web of Science ®Google Scholar
• Tomkinson, B., and Kieff, E.. 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
   PubMedGoogle Scholar
• Tomkinson, B., Robertson, E., and Kieff, E.. 1993. Epstein-Barr virus nuclear proteins EBNA-3A and EBNA-3C are essential for B-lymphocyte growth transformation. J. Virol. 67:2014–2025
   PubMed Web of Science ®Google Scholar
• Tsitsiloni, O. E., Stiakakis, J., Koutselinis, A., Gogas, J., Markopoulos, C., Yialouris, P., Bekris, S., Panoussopoulos, D., Kiortsis, V., Voelter, W. et al. 1993. Expression of alpha-thymosins in human tissues in normal and abnormal growth. Proc. Natl. Acad. Sci. USA 90:9504–9507
   PubMed Web of Science ®Google Scholar
• Vareli, K., Frangou-Lazaridis, M., and Tsolas, O.. 1995. Prothymosin alpha mRNA levels vary with c-myc expression during tissue proliferation, viral infection and heat shock. FEBS Lett. 371:337–340
   PubMedGoogle Scholar
• Vareli, K., Tsolas, O., and Frangou-Lazaridis, M.. 1996. Regulation of prothymosin alpha during the cell cycle. Eur. J. Biochem. 238:799–806
   PubMedGoogle Scholar
• Wang, F., Kikutani, H., Tsang, S. F., Kishimoto, T., and Kieff, E.. 1991. Epstein-Barr virus nuclear protein 2 transactivates a cis-acting CD23 DNA element. J. Virol. 65:4101–4106
   PubMedGoogle Scholar
• Wang, F., Tsang, S. F., Kurilla, M. G., Cohen, J. I., and Kieff, E.. 1990. Epstein-Barr virus nuclear antigen 2 transactivates latent membrane protein LMP1. J. Virol. 64:3407–3416
   PubMed Web of Science ®Google Scholar
• Wang, L., Grossman, S. R., and Kieff, E.. 2000. Epstein-Barr virus nuclear protein 2 interacts with p300, CBP, and PCAF histone acetyltransferases in activation of the LMP1 promoter. Proc. Natl. Acad. Sci. USA 97:430–435
   PubMed Web of Science ®Google Scholar
• Weintraub, H.. 1984. Histone-H1-dependent chromatin superstructures and the suppression of gene activity. Cell 38:17–27
   PubMed Web of Science ®Google Scholar
• Wu, C. L., Shiau, A. L., and Lin, C. S.. 1997. Prothymosin alpha promotes cell proliferation in NIH3T3 cells. Life Sci. 61:2091–2101
   PubMedGoogle Scholar
• Yalamanchili, R., Tong, X., Grossman, S., Johannsen, E., Mosialos, G., and Kieff, E.. 1994. Genetic and biochemical evidence that EBNA 2 interaction with a 63-kDa cellular GTG-binding protein is essential for B lymphocyte growth transformation by EBV. Virology 204:634–641
   PubMedGoogle Scholar
• Yang, X. J., Ogryzko, V. V., Nishikawa, J., Howard, B. H., and Nakatani, Y.. 1996. A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature 382:319–324
   PubMed Web of Science ®Google Scholar
• Yates, J., Warren, N., Reisman, D., and Sugden, B.. 1984. A cis-acting element from the Epstein-Barr viral genome that permits stable replication of recombinant plasmids in latently infected cells. Proc. Natl. Acad. Sci. USA 81:3806–3810
   PubMed Web of Science ®Google Scholar
• Zhao, B., Marshall, D. R., and Sample, C. E.. 1996. A conserved domain of the Epstein-Barr virus nuclear antigens 3A and 3C binds to a discrete domain of Jκ. J. Virol. 70:4228–4236
   PubMed Web of Science ®Google Scholar
• Zimber-Strobl, U., Strobl, L. J., Meitinger, C., Hinrichs, R., Sakai, T., Furukawa, T., Honjo, T., and Bornkamm, G. W.. 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
   PubMedGoogle Scholar