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PMID: 7724549 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

The 62- and 80-kDa subunits of transcription factor IIH mediate the interaction with Epstein-Barr virus nuclear protein 2.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 92 ·No. 8 ·1995-04-11 ·Pages 3259-63

Tong X, Drapkin R, Reinberg D, Kieff E

Abstract

EBNA 2 (Epstein-Barr virus nuclear antigen 2) is an acidic transactivator essential for EBV transformation of B lymphocytes. We show that EBNA 2 directly interacts with general transcription factor IIH. Glutathione S-transferase (GST)-EBNA 2 acidic domain fusion protein depleted transcription factor IIH activity from a TFIIH nuclear fraction. The p89 (ERCC3), p80 (ERCC2), and p62 subunits of TFIIH were among the proteins retained by GST-EBNA 2. Eluates from the GST-EBNA 2 beads reconstituted activity in a TFIIH-dependent in vitro transcription assay. The p62 and p80 subunits of TFIIH independently bound to GST-EBNA 2, whereas the p34 subunit of TFIIH only bound in the presence of p62. A Trp-->Thr mutation in the EBNA 2 acidic domain abolishes EBNA 2 transactivation in vivo and greatly compromised EBNA 2 association with TFIIH activity and with the p62 and p80 subunits, providing a link between EBNA 2 transactivation and these interactions. Antibodies directed against the p62 subunit of TFIIH coimmunoprecipitated EBNA 2 from EBV-transformed B lymphocytes, indicating that EBNA 2 associates with TFIIH in vivo.

MeSH Terms
Adenosine Triphosphatases/metabolism Antigens, Viral/genetics,metabolism B-Lymphocytes/metabolism Cell Nucleus/metabolism Cells, Cultured DNA Helicases/metabolism DNA Mutational Analysis DNA-Binding Proteins/genetics,metabolism Epstein-Barr Virus Nuclear Antigens Protein Binding Protein Conformation Protein Kinases/metabolism Recombinant Fusion Proteins/metabolism Structure-Activity Relationship Transcription Factor TFIIH Transcription Factors/metabolism Transcription Factors, TFII Transcription, Genetic Transcriptional Activation
Chemicals
Antigens, Viral DNA-Binding Proteins Epstein-Barr Virus Nuclear Antigens Recombinant Fusion Proteins Transcription Factors Transcription Factors, TFII Transcription Factor TFIIH Protein Kinases Adenosine Triphosphatases DNA Helicases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Tong X
Department of Medicine and Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115, USA.
Drapkin R
Reinberg D
Kieff E
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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.92.8.3259
Published
1995-04-11
Pages
3259-63
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC42145
Subset
IM
Grants
NCI NIH HHS · CA 47006 · United States
NIGMS NIH HHS · GM08360 · United States
NIGMS NIH HHS · GM37120 · United States
External Links
PubMed source DOI: 10.1073/pnas.92.8.3259 PMC Full Text View journal details
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