1: Eur J Neurosci. 2001 Oct;14(8):1303-12. 

Biological activity of RE-1 silencing transcription factor (REST) towards
distinct transcriptional activators.

Lietz M, Bach K, Thiel G.

Department of Medical Biochemistry and Molecular Biology, University of Saarland
Medical Center, D-66421 Homburg, Germany.

The zinc finger protein RE-1 silencing transcription factor (REST) is a
transcriptional repressor that represses neuronal genes in non-neuronal tissues.
We have analyzed the ability of REST and the REST mutants, RESTDeltaN and
RESTDeltaC lacking either the N-terminal or C-terminal repression domains of
REST, to inhibit transcription mediated by distinct transcriptional activator
proteins. For this purpose we have designed an activator specific assay where
transcription is activated as a result of only one distinct activation domain.
In addition, binding sites for REST were inserted in the 5'-untranslated region
or at a distant position downstream of the polyadenylation signal. The results
show that REST or the REST mutants containing only one repression domain were
able to block transcriptional activation mediated by the transcriptional
activation domains derived from p53, AP2, Egr-1, and GAL4. Moreover, REST, as
well as the REST mutants, blocked the activity of the phosphorylation-dependent
activation domain of Elk1. However, the activity of the activation domain
derived from cAMP response element binding protein 2 (CREB2), was not inhibited
by REST, RESTDeltaN or RESTDeltaC, suggesting that REST is able to distinguish
between distinct transcriptional activation domains. Additionally, the activator
specific assay, together with a positive-dominant mutant of REST that activated
instead of repressed transcription, was used in titration experiments to show
that REST has transcriptional repression and no transcriptional activation
properties when bound to the 5'-untranslated region of a gene.

PMID: 11703459 [PubMed - indexed for MEDLINE]


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