The CtBP binding domain in the adenovirus E1A protein controls CR1-dependent transactivation.
AUTOR(ES)
Sollerbrant, K
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=145971Documentos Relacionados
- Acetylation of adenovirus E1A regulates binding of the transcriptional corepressor CtBP
- Multiple transcription factor binding sites mediate adenovirus E1A transactivation.
- Overlapping and Unique Roles for C-Terminal Binding Protein 1 (CtBP1) and CtBP2 during Mouse Development.
- BS69, a novel adenovirus E1A-associated protein that inhibits E1A transactivation.
- CtBP Contributes Quantitatively to Knirps Repression Activity in an NAD Binding-Dependent Manner