A conserved region of unknown function participates in the recognition of E2F family members by the adenovirus E4 ORF 6/7 protein

Christine A. Jost, Doron Ginsberg, William G. Kaelin

Research output: Contribution to journalArticlepeer-review

15 Scopus citations

Abstract

E2F DNA-binding activity in vivo is due to heterodimer formation between members of the E2F and DP transcription factor families. The ability of these heterodimers to serve as transcriptional regulators is modulated by complex formation with additional proteins such as the products of the retinoblastoma gene and the adenovirus E4 ORF 6/7. Each of the E2F family members cloned to date contains a highly conserved region of unknown function, termed the marked box, which lies between their DNA binding and transactivation domains. Mutational analysis showed that the marked box contributed to the recognition of E2F family members by the E4 ORF 6/7 protein in vitro and in vivo.

Original languageEnglish
Pages (from-to)78-90
Number of pages13
JournalVirology
Volume220
Issue number1
DOIs
StatePublished - 1 Jun 1996
Externally publishedYes

Bibliographical note

Funding Information:
We thank Suman Shirodkar for advice on performing the gel-shift assays, Willy Krek for the E2F2 and E2F3 expression plasmids, Claude Sardet for the E2F5 cDNA, Joseph Nevins for the E4 plasmids used in this study, and Patrick Hearing for the E4 antibody. We also thank our colleagues in the Kaelin laboratory for many helpful discussions and for their critical reading of this manuscript. This work was supported by the Sandoz Research Institute and an NIH Physcian-Scientist Award (W.G.K.). W.G.K. is a McDonnell Foundation Scholar.

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