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PMID: 8052621 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

The Epstein-Barr virus nuclear antigen 2 transactivator is directed to response elements by the J kappa recombination signal binding protein.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 91 ·No. 16 ·1994-08-02 ·Pages 7568-72

Grossman SR, Johannsen E, Tong X, Yalamanchili R, Kieff E

Abstract

Epstein-Barr virus nuclear antigen 2 (EBNA-2) plays an essential role in primary B-lymphocyte growth transformation. EBNA-2 is an acidic transcriptional transactivator that is brought to virus and cell EBNA-2 response elements by interaction with a factor that recognizes the double-stranded sequence MNYYGTGGGAA, where M is A or C, N is any nucleotide, and Y is a pyrimidine. A 63-kDa protein that recognizes this DNA sequence has now been purified by S-Sepharose and oligonucleotide affinity chromatography. p63 peptide sequence is identical to the predicted amino acid sequence for the human J kappa immunoglobulin recombination signal binding protein. Purified or recombinant in vitro-translated J kappa binds to the MNYYGTGGGAA EBNA-2 response element sequence and interacts with EBNA-2. Surprisingly, J kappa does not bind to the J kappa 1 heptamer recombination signal sequence (CACTGTG), and its prior identification as a heptamer binding protein was most likely due to the addition of a BamHI restriction site to the native heptamer creating a near EBNA-2 response element consensus (CACTGTGGGAT).

MeSH Terms
Amino Acid Sequence Antigens, Viral/metabolism B-Lymphocytes/metabolism Base Sequence DNA-Binding Proteins/genetics,metabolism Epithelium/metabolism Epstein-Barr Virus Nuclear Antigens Herpesvirus 4, Human/genetics Molecular Sequence Data Nuclear Proteins/metabolism Protein Binding Recombinant Proteins/metabolism Recombination, Genetic Regulatory Sequences, Nucleic Acid/genetics T-Lymphocytes/metabolism
Chemicals
Antigens, Viral DNA-Binding Proteins Epstein-Barr Virus Nuclear Antigens Nuclear Proteins Recombinant Proteins
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Grossman S R
Department of Medicine, Harvard Medical School, Boston, MA 02115.
Johannsen E
Tong X
Yalamanchili R
Kieff E
References (32)
32 references, click to expand
  1. Epstein-Barr virus nuclear antigen 2 specifically induces expression of the B-cell activation antigen CD23.
    Proc Natl Acad Sci U S A. 1987 May;84(10):3452-6 PMID: 3033649
  2. Affinity purification of sequence-specific DNA binding proteins.
    Proc Natl Acad Sci U S A. 1986 Aug;83(16):5889-93 PMID: 3461465
  3. GAL4-VP16 is an unusually potent transcriptional activator.
    Nature. 1988 Oct 6;335(6190):563-4 PMID: 3047590
  4. Influence of Burkitt's lymphoma and primary B cells on latent gene expression by the nonimmortalizing P3J-HR-1 strain of Epstein-Barr virus.
    J Virol. 1989 Apr;63(4):1531-9 PMID: 2538644
  5. Genetic analysis of immortalizing functions of Epstein-Barr virus in human B lymphocytes.
    Nature. 1989 Aug 3;340(6232):393-7 PMID: 2547164
  6. The Oct-1 homoeodomain directs formation of a multiprotein-DNA complex with the HSV transactivator VP16.
    Nature. 1989 Oct 19;341(6243):624-30 PMID: 2571937
  7. Purification and characterization of a protein that binds to the recombination signal sequence of the immunoglobulin J kappa segment.
    Nucleic Acids Res. 1989 Nov 25;17(22):9015-26 PMID: 2511556
  8. The octamer-binding proteins form multi-protein--DNA complexes with the HSV alpha TIF regulatory protein.
    EMBO J. 1989 Dec 20;8(13):4229-38 PMID: 2556266
  9. 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
  10. Epstein-Barr virus nuclear protein 2 is a key determinant of lymphocyte transformation.
    Proc Natl Acad Sci U S A. 1989 Dec;86(23):9558-62 PMID: 2556717
  11. Epstein-Barr virus nuclear antigen 2 transactivates latent membrane protein LMP1.
    J Virol. 1990 Jul;64(7):3407-16 PMID: 2352328
  12. Identification of cellular proteins that can interact specifically with the T/E1A-binding region of the retinoblastoma gene product.
    Cell. 1991 Feb 8;64(3):521-32 PMID: 1825028
  13. Early events in Epstein-Barr virus infection of human B lymphocytes.
    Virology. 1991 Apr;181(2):595-608 PMID: 1849678
  14. Hairless is required for the development of adult sensory organ precursor cells in Drosophila.
    Development. 1991 Jan;111(1):89-104 PMID: 2015800
  15. Epstein-Barr virus nuclear protein 2 mutations define essential domains for transformation and transactivation.
    J Virol. 1991 May;65(5):2545-54 PMID: 1850028
  16. Epstein-Barr virus nuclear protein 2 transactivates a cis-acting CD23 DNA element.
    J Virol. 1991 Aug;65(8):4101-6 PMID: 1649318
  17. An Epstein-Barr virus nuclear protein 2 domain essential for transformation is a direct transcriptional activator.
    J Virol. 1991 Nov;65(11):5880-5 PMID: 1656076
  18. Delineation of the cis-acting element mediating EBNA-2 transactivation of latent infection membrane protein expression.
    J Virol. 1991 Dec;65(12):6765-71 PMID: 1658373
  19. The Drosophila RBP-J kappa gene encodes the binding protein for the immunoglobulin J kappa recombination signal sequence.
    J Biol Chem. 1991 Dec 5;266(34):23334-40 PMID: 1744127
  20. Amino acids necessary for DNA contact and dimerization imply novel motifs in the papillomavirus E2 trans-activator.
    Genes Dev. 1992 Jan;6(1):105-16 PMID: 1309714
  21. Genomic organization of mouse J kappa recombination signal binding protein (RBP-J kappa) gene.
    J Biol Chem. 1992 Feb 25;267(6):4016-22 PMID: 1740450
  22. Identification of critical cis elements involved in mediating Epstein-Barr virus nuclear antigen 2-dependent activity of an enhancer located upstream of the viral BamHI C promoter.
    J Virol. 1992 May;66(5):2846-52 PMID: 1313905
  23. 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
  24. Crystal structure at 1.7 A of the bovine papillomavirus-1 E2 DNA-binding domain bound to its DNA target.
    Nature. 1992 Oct 8;359(6395):505-12 PMID: 1328886
  25. 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
  26. The Epstein-Barr virus nuclear antigen 2 interacts with an EBNA2 responsive cis-element of the terminal protein 1 gene promoter.
    EMBO J. 1993 Jan;12(1):167-75 PMID: 8381349
  27. Epstein-Barr virus-induced genes: first lymphocyte-specific G protein-coupled peptide receptors.
    J Virol. 1993 Apr;67(4):2209-20 PMID: 8383238
  28. Cell phenotype-dependent control of Epstein-Barr virus latent membrane protein 1 gene regulatory sequences.
    Virology. 1993 Jul;195(1):71-80 PMID: 8391188
  29. Human Jk recombination signal binding protein gene (IGKJRB): comparison with its mouse homologue.
    Genomics. 1993 Aug;17(2):306-15 PMID: 8406481
  30. 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
  31. The genetics of a small autosomal region of Drosophila melanogaster containing the structural gene for alcohol dehydrogenase. III. Hypomorphic and hypermorphic mutations affecting the expression of hairless.
    Genetics. 1982 Jul-Aug;101(3-4):447-59 PMID: 6816670
  32. Trans-acting protein factors and the regulation of eukaryotic transcription: lessons from studies on DNA tumor viruses.
    Genes Dev. 1988 Mar;2(3):267-81 PMID: 3288540
Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.91.16.7568
Published
1994-08-02
Pages
7568-72
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC44443
Subset
IM
Grants
NIAID NIH HHS · AI08548-02 · United States
External Links
PubMed source DOI: 10.1073/pnas.91.16.7568 PMC Full Text View journal details
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