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

被引:95
作者
Trouche, D
Kouzarides, T
机构
[1] UNIV CAMBRIDGE,WELLCOME CANC RES CAMPAIGN INST,CAMBRIDGE CB2 1QR,ENGLAND
[2] UNIV CAMBRIDGE,DEPT PATHOL,CAMBRIDGE CB2 1QR,ENGLAND
基金
英国惠康基金;
关键词
D O I
10.1073/pnas.93.4.1439
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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 RE and CBP/p300 proteins, which are preserved in the same relative order along F2F1 and E1A, Furthermore, the interaction of RE and CBP with these two activation domains results in the same functional consequences: RE 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.
引用
收藏
页码:1439 / 1442
页数:4
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