Nucleic Acids Research, Vol 25, Issue 18 3621-3628, Copyright © 1997 by Oxford University Press
Y Katan, R Agami and Y Shaul
EP is a DNA element found in regulatory regions of viral and cellular
genes. While being a key functional element in viral enhancers, EP has no
intrinsic enhancer activity but can stimulate or silence transcription in a
context-dependent manner. The EP element is bound by RFX1, which belongs to
a novel, evolutionarily conserved protein family. In an attempt to decipher
the mechanism by which EP regulates transcription, the intrinsic
transcriptional activity of RFX1 was investigated. A functional dissection
of RFX1, by analysis of deletion mutants and chimeric proteins, identified
several regions with independent transcriptional activity. An activation
domain containing a glutamine-rich region is found in the N-terminal half
of RFX1, while a region with repressor activity overlaps the C-terminal
dimerization domain. In RFX1 these activities were mutually neutralized,
producing a nearly inactive transcription factor. This neutralization
effect was reproduced by fusing RFX1 sequences to a heterologous
DNA-binding domain. We propose that relief of self-neutralization may allow
RFX1 to act as a dual-function regulator via its activation and repression
domains, accounting for the context-dependent activity of EP.
ARTICLES
The transcriptional activation and repression domains of RFX1, a context-dependent regulator, can mutually neutralize their activities
Department of Molecular Genetics, The Weizmann Institute of Science, Rehovot 76100, Israel.
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