E2F1 and E1A(12S) have a homologous activation domain regulated by RB and CBP.

Abstract:

:The E2F1 transcription factor has a well-characterized activation domain at its C terminus and the E1A protein has a recently defined activation domain at its N terminus. Here we show that these activation domains are highly related in sequence. The sequence homology reflects, at least partly, the conservation of common binding sites for the RB and CBP/p300 proteins, which are preserved in the same relative order along E2F1 and E1A. Furthermore, the interaction of RB and CBP with these two activation domains results in the same functional consequences: RB represses both activation domains, whereas CBP stimulates them. We conclude that the activation domains of E1A(12s) and E2F1 belong to a novel functional class, characterized by specific protein binding sites. The implication of this conservation with respect to E1A-induced stimulation of E2F activity is discussed.

authors

Trouche D,Kouzarides T

doi

10.1073/pnas.93.4.1439

subject

Has Abstract

pub_date

1996-02-20 00:00:00

pages

1439-42

issue

4

eissn

0027-8424

issn

1091-6490

journal_volume

93

pub_type

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