Home LiteratureArticle Details
PMID: 8648764 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

EBNA-2 and EBNA-3C extensively and mutually exclusively associate with RBPJkappa in Epstein-Barr virus-transformed B lymphocytes.

Journal of virology ·Vol. 70 ·No. 6 ·1996-06-00 ·Pages 4179-83

Johannsen E, Miller CL, Grossman SR, Kieff E

Abstract

Although genetic and biochemical data indicate that the cell protein RBPJkappa is a mediator of EBNA-2 and EBNA-3C effects on transcriptional regulatory elements, the extent of association of these Epstein-Barr virus nuclear proteins with RBPJkappa in transformed B lymphocytes has not been determined. We now report that most of the EBNA-2 and at least 20% of the EBNA-3C coimmunoprecipitated with RBPJkappa from extracts of transformed B lymphocytes that contained most of the cellular EBNA-2 and EBNA3C. Both proteins are associated preferentially with the smaller of the two RBPJkappa isoforms. EBNA-2-RBPJkappa complexes do not contain EBNA-3C, and EBNA-3C-RBPJkappa complexes do not contain EBNA-2. Although EBNA-2 and EBNA-3C are extensively associated with RBPJkappa, a fraction of RBPJkappa appears to be free of EBNAs after repeated immunoprecipitations with anti-EBNA, Epstein-Barr virus-immune, human antibody. Promoters with RBPJkappa sites in their regulatory elements are likely to be differentially regulated by these RBPJkappa-EBNA-2 and RBPJkappa-EBNA-3 complexes.

MeSH Terms
Antigens, Viral/metabolism B-Lymphocytes/immunology DNA-Binding Proteins/metabolism Epstein-Barr Virus Nuclear Antigens Herpesvirus 4, Human/physiology Humans Immunoglobulin J Recombination Signal Sequence-Binding Protein Lymphocyte Activation Nuclear Proteins Precipitin Tests
Chemicals
Antigens, Viral DNA-Binding Proteins Epstein-Barr Virus Nuclear Antigens Immunoglobulin J Recombination Signal Sequence-Binding Protein Nuclear Proteins RBPJ protein, human
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Johannsen E
Department of Microbiology and Molecular Genetics, Harvard University, Boston, Massachusetts 02115, USA.
Miller C L
Grossman S R
Kieff E
References (44)
44 references, click to expand
  1. Notch is required for wingless signaling in the epidermis of Drosophila.
    Cell. 1994 Oct 21;79(2):259-72 PMID: 7954794
  2. The amino-terminal domains of Epstein-Barr virus nuclear proteins 3A, 3B, and 3C interact with RBPJ(kappa).
    J Virol. 1996 May;70(5):3068-74 PMID: 8627785
  3. 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. 1994 Oct 17;13(20):4973-82 PMID: 7957063
  4. 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. 1994 Oct 15;8(20):2491-503 PMID: 7958912
  5. 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. 1994 Dec;205(2):596-602 PMID: 7975264
  6. Immortalization of human B lymphocytes by a plasmid containing 71 kilobase pairs of Epstein-Barr virus DNA.
    J Virol. 1995 Jan;69(1):231-8 PMID: 7983714
  7. Epstein-Barr virus nuclear protein 2 transactivation of the latent membrane protein 1 promoter is mediated by J kappa and PU.1.
    J Virol. 1995 Jan;69(1):253-62 PMID: 7983717
  8. The Epstein-Barr virus nuclear protein 2 acidic domain can interact with TFIIB, TAF40, and RPA70 but not with TATA-binding protein.
    J Virol. 1995 Jan;69(1):585-8 PMID: 7983760
  9. The Spi-1/PU.1 and Spi-B ets family transcription factors and the recombination signal binding protein RBP-J kappa interact with an Epstein-Barr virus nuclear antigen 2 responsive cis-element.
    EMBO J. 1994 Dec 1;13(23):5624-32 PMID: 7988559
  10. Epstein-Barr virus nuclear protein 3C modulates transcription through interaction with the sequence-specific DNA-binding protein J kappa.
    J Virol. 1995 May;69(5):3108-16 PMID: 7707539
  11. Notch signaling.
    Science. 1995 Apr 14;268(5208):225-32 PMID: 7716513
  12. Subnuclear localization and phosphorylation of Epstein-Barr virus latent infection nuclear proteins.
    Virology. 1990 Jun;176(2):563-74 PMID: 2161150
  13. Epstein-Barr virus nuclear antigen 2 transactivates latent membrane protein LMP1.
    J Virol. 1990 Jul;64(7):3407-16 PMID: 2352328
  14. Epstein-Barr virus nuclear protein 2 mutations define essential domains for transformation and transactivation.
    J Virol. 1991 May;65(5):2545-54 PMID: 1850028
  15. TAN-1, the human homolog of the Drosophila notch gene, is broken by chromosomal translocations in T lymphoblastic neoplasms.
    Cell. 1991 Aug 23;66(4):649-61 PMID: 1831692
  16. 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. 1992 May;66(5):2893-903 PMID: 1313908
  17. The Drosophila homolog of the immunoglobulin recombination signal-binding protein regulates peripheral nervous system development.
    Cell. 1992 Jun 26;69(7):1191-7 PMID: 1617729
  18. Suppressor of Hairless, the Drosophila homolog of the mouse recombination signal-binding protein gene, controls sensory organ cell fates.
    Cell. 1992 Jun 26;69(7):1199-212 PMID: 1617730
  19. Biochemical and immunological characterization of the DNA binding protein (RBP-J kappa) to mouse J kappa recombination signal sequence.
    J Biochem. 1992 Sep;112(3):314-20 PMID: 1429518
  20. Epstein-Barr virus nuclear proteins EBNA-3A and EBNA-3C are essential for B-lymphocyte growth transformation.
    J Virol. 1993 Apr;67(4):2014-25 PMID: 8445720
  21. Human Jk recombination signal binding protein gene (IGKJRB): comparison with its mouse homologue.
    Genomics. 1993 Aug;17(2):306-15 PMID: 8406481
  22. The Epstein-Barr virus immortalizing protein EBNA-2 is targeted to DNA by a cellular enhancer-binding protein.
    Proc Natl Acad Sci U S A. 1993 Oct 15;90(20):9237-41 PMID: 8415684
  23. Precipitation of the Epstein-Barr virus protein EBNA 2 by an EBNA 3c-specific monoclonal antibody.
    J Gen Virol. 1994 Apr;75 ( Pt 4):769-78 PMID: 7512118
  24. The recombination signal sequence-binding protein RBP-2N functions as a transcriptional repressor.
    Mol Cell Biol. 1994 May;14(5):3310-9 PMID: 8164682
  25. Epstein-Barr virus nuclear antigen EBNA3C/6 expression maintains the level of latent membrane protein 1 in G1-arrested cells.
    J Virol. 1994 Jun;68(6):3491-8 PMID: 8189488
  26. Modulation of vimentin, the CD40 activation antigen and Burkitt's lymphoma antigen (CD77) by the Epstein-Barr virus nuclear antigen EBNA-4.
    Virology. 1994 Jul;202(1):16-24 PMID: 8009829
  27. Mediation of Epstein-Barr virus EBNA2 transactivation by recombination signal-binding protein J kappa.
    Science. 1994 Jul 1;265(5168):92-5 PMID: 8016657
  28. 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. 1994 Nov 1;204(2):634-41 PMID: 7941331
  29. A second nuclear protein is encoded by Epstein-Barr virus in latent infection.
    Science. 1985 Mar 8;227(4691):1238-40 PMID: 2983420
  30. Monoclonal and polyclonal antibodies against Epstein-Barr virus nuclear antigen 5 (EBNA-5) detect multiple protein species in Burkitt's lymphoma and lymphoblastoid cell lines.
    J Virol. 1987 Dec;61(12):3870-8 PMID: 2824821
  31. Genetic analysis of immortalizing functions of Epstein-Barr virus in human B lymphocytes.
    Nature. 1989 Aug 3;340(6232):393-7 PMID: 2547164
  32. Expression of Epstein-Barr virus transformation-associated genes in tissues of patients with EBV lymphoproliferative disease.
    N Engl J Med. 1989 Oct 19;321(16):1080-5 PMID: 2552313
  33. A protein binding to the J kappa recombination sequence of immunoglobulin genes contains a sequence related to the integrase motif.
    Nature. 1989 Dec 21-28;342(6252):934-7 PMID: 2556644
  34. Aspartic acid-96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsin.
    Proc Natl Acad Sci U S A. 1989 Dec;86(23):9228-32 PMID: 2556706
  35. Epstein-Barr virus nuclear antigen 2 induces expression of the virus-encoded latent membrane protein.
    J Virol. 1990 May;64(5):2126-34 PMID: 2157875
  36. 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. 1990 May;64(5):2309-18 PMID: 2157887
  37. The 62- and 80-kDa subunits of transcription factor IIH mediate the interaction with Epstein-Barr virus nuclear protein 2.
    Proc Natl Acad Sci U S A. 1995 Apr 11;92(8):3259-63 PMID: 7724549
  38. Epstein-Barr virus nuclear antigen 3C is a transcriptional regulator.
    J Virol. 1995 Jun;69(6):3624-30 PMID: 7745710
  39. The Epstein-Barr virus nuclear protein 2 acidic domain forms a complex with a novel cellular coactivator that can interact with TFIIE.
    Mol Cell Biol. 1995 Sep;15(9):4735-44 PMID: 7651391
  40. Signal transduction. Notch takes a short cut.
    Nature. 1995 Sep 28;377(6547):288-9 PMID: 7566081
  41. Signalling downstream of activated mammalian Notch.
    Nature. 1995 Sep 28;377(6547):355-8 PMID: 7566092
  42. The neurogenic suppressor of hairless DNA-binding protein mediates the transcriptional activation of the enhancer of split complex genes triggered by Notch signaling.
    Genes Dev. 1995 Nov 1;9(21):2598-608 PMID: 7590238
  43. The N-terminal half of EBNA2, except for seven prolines, is not essential for primary B-lymphocyte growth transformation.
    J Virol. 1996 Apr;70(4):2468-73 PMID: 8642674
  44. The suppressor of hairless protein participates in notch receptor signaling.
    Cell. 1994 Oct 21;79(2):273-82 PMID: 7954795
Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
DOI
10.1128/JVI.70.6.4179-4183.1996
Published
1996-06-00
Pages
4179-83
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC190314
Subset
IM
Grants
NIAID NIH HHS · AI07245 · United States
NCI NIH HHS · CA47006 · United States
External Links
PubMed source DOI: 10.1128/JVI.70.6.4179-4183.1996 PMC Full Text View journal details
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: [email protected]

Copyright © 2026.Genelibs Jinan Honghui Biotechnology Co., Ltd. 鲁ICP备20007159号-2