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J Biol Chem, Vol. 273, Issue 29, 18086-18091, July 17, 1998
From the Department of Molecular Genetics, Albert Einstein College
of Medicine, Bronx, New York 10461
The ZFM1 protein is both a transcriptional
repressor and identical to the splicing factor SF1. ZFM1 was shown to
interact with and repress transcription from the glycine, glutamine,
serine, and threonine-rich transcription activation domain of the sea urchin transcription factor, stage-specific activator protein (SSAP).
EWS, a human protein involved in cellular transformation in Ewing's
sarcoma tumors, contains an NH2-terminal
transcriptional activation domain (NTD) which resembles that of SSAP in
both amino acid composition and the ability to drive transcription to
levels higher than VP16 in most cell types. Here we report that ZFM1 also interacts with EWS in both two-hybrid assays and glutathione S-transferase pull-down experiments. The region on EWS
which interacts with ZFM1 maps to 37 amino acids within its NTD.
Overexpression of ZFM1 in HepG2 cells represses the transactivation of
reporter gene expression driven by Gal4-EWS-NTD fusion protein and this repression correlates with ZFM1 binding to EWS. Furthermore, two proteins, TLS and hTAFII68, which have extensive homology
to EWS, also interact with ZFM1. Recently, it was discovered that
EWS/TLS/hTAFII68 are each present in distinct TFIID
populations and EWS and hTAFII68 were also found to be
associated with the RNA polymerase II holoenzyme. The association of
ZFM1 with these proteins implies that one normal cellular function for
ZFM1 may be to negatively modulate transcription of target genes
coordinated by these cofactors.
The Transcriptional Repressor ZFM1 Interacts with and Modulates
the Ability of EWS to Activate Transcription
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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