Cloning and characterization of E2F-2, a novel protein with the biochemical properties of transcription factor E2F
Cloning and characterization of E2F-2, a novel protein with the biochemical properties of transcription factor E2F
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DOI:
10.1128/mcb.13.12.7802-7812.1993
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发表时间:
1993-12
影响因子:
5.3
通讯作者:
M. Ivey-Hoyle;R. Conroy;H. Huber;P. Goodhart;A. Oliff;D. Heimbrook
中科院分区:
文献类型:
--
作者:
M. Ivey-Hoyle;R. Conroy;H. Huber;P. Goodhart;A. Oliff;D. Heimbrook
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.