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Nucleic Acids Res. 1996 Jul 1;24(13):2578-84.

The CtBP binding domain in the adenovirus E1A protein controls CR1-dependent transactivation.

Author information

1
Department of Cell and Molecular Biology, Karolinska Institutet, Stockholm, Sweden.

Abstract

The adenovirus E1A-243R protein has the ability to force a resting cell into uncontrolled proliferation by modulating the activity of key targets in cell cycle control. Most of these regulatory mechanisms are dependent on activities mapping to conserved region 1 (CR1) and the non-conserved N-terminal region of E1A. We have previously shown that CR1 functions as a very patent transactivator when it is tethered to a promoter through a heterologous DNA binding domain. However, artificial DNA binding was not sufficient to convert full-length E1A-243R to a transactivator. Thus, an additional function(s) of the E1A-243R protein modulates the effect of CR1 in transcription regulation. Here we demonstrate that a 44 amino acid region at the extreme C-terminus of ElA inhibited transactivation by a Gal4-CR1 fusion protein. Inhibition correlated with binding of the nuclear 48 kDa C-terminal binding protein (CtBP), which has been implicated in E1A-mediated suppression of the metastazing potential of tumour cells. This might suggest that CtBP binding can regulate E1A-mediated transformation by modulating CR1-dependent control of transcription.

PMID:
8692699
PMCID:
PMC145971
DOI:
10.1093/nar/24.13.2578
[Indexed for MEDLINE]
Free PMC Article

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