CLONING AND CHARACTERIZATION OF E2F-2, A NOVEL PROTEIN WITH THE BIOCHEMICAL-PROPERTIES OF TRANSCRIPTION FACTOR-E2F

被引:198
作者
IVEYHOYLE, M [1 ]
CONROY, R [1 ]
HUBER, HE [1 ]
GOODHART, PJ [1 ]
OLIFF, A [1 ]
HEIMBROOK, DC [1 ]
机构
[1] MERCK RES LABS,DEPT CANC RES,W POINT,PA 19486
关键词
D O I
10.1128/MCB.13.12.7802
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
E2F is a mammalian transcription factor that appears to play an important role in cell cycle regulation. While at least two proteins (E2F-1 and DP-1) with E2F-like activity have been cloned, studies from several laboratories suggest that additional homologs may exist. A novel protein with E2F-like properties, designated E2F-2, was cloned by screening a HeLa cDNA library with a DNA probe derived from the DNA binding domain of E2F-1 (K. Helin, J. A. Lees, M. Vidal, N. Dyson, E. Harlow, and A. Fattaey, Cell 70:337-350, 1992). E2F-2 exhibits overall 46% amino acid identity to E2F-1. Both the sequence and the function of the DNA and retinoblastoma gene product binding domains of E2F-1 are conserved in E2F-2. The DNA binding activity of E2F-2 is dramatically enhanced by complementation with particular sodium dodecyl sulfate-polyacrylamide gel electrophoresis-purified components of HeLa cell E2F, and anti-E2F-2 antibodies cross-react with components of purified HeLa cell E2F. These observations are consistent with a model in which E2F binds DNA as a heterodimer of two distinct proteins, and E2F-2 is functionally and immunologically related to one of these proteins.
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页码:7802 / 7812
页数:11
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