The Epstein-Barr virus nuclear protein 2 acidic domain can interact with TFIIB, TAF40, and RPA70 but not with TATA-binding protein.

Abstract:

:The Epstein-Barr virus nuclear antigen 2 (EBNA-2) acidic domain is essential for B-lymphocyte growth transformation and can activate transcription when brought to a promoter by a sequence-specific DNA-binding domain. We now show that the EBNA-2 acidic domain has slightly less activity than the proteotypic acidic transactivator VP16 in depleting nuclear extracts of basal transcription activity. Like VP16, EBNA-2 associates with TFIIB, TAF40, and RPA70. However, EBNA-2 has much less avidity for TATA-binding protein. A Trp-to-Thr mutation within the acidic domain abolishes EBNA-2 transactivating activity and greatly compromises the association with TFIIB, TAF40, and RPA70, establishing a genetic linkage between transactivating activity and these associations.

journal_name

J Virol

journal_title

Journal of virology

authors

Tong X,Wang F,Thut CJ,Kieff E

doi

10.1128/JVI.69.1.585-588.1995

subject

Has Abstract

pub_date

1995-01-01 00:00:00

pages

585-8

issue

1

eissn

0022-538X

issn

1098-5514

journal_volume

69

pub_type

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