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Vol. 273, Issue 1, 484-494, January 2, 1998
From the We have previously identified a muscle-specific
enhancer within the first intron of the human
Negative Regulation of
Enolase Gene Transcription in
Embryonic Muscle Is Dependent upon a Zinc Finger Factor That Binds to
the G-rich Box within the Muscle-specific Enhancer
,,,
,,
Istituto di Biologia dello Sviluppo del
Consiglio Nazionale delle Ricerche, Via Ugo La Malfa 153, 90146 Palermo, Italy, the ¶ Dipartimento di Biologia
Cellulare e dello Sviluppo, Università di Palermo, 90128 Palermo,
Italy, and the Dipartimento di Istologia ed Embriologia Medica,
Università di Roma La Sapienza, 00161 Roma, Italy
enolase gene. Present
in this enhancer are an A/T-rich box that binds MEF-2 protein(s) and a G-rich box (AGTGGGGGAGGGGGCTGCG) that interacts with ubiquitously expressed factors. Both elements are required for tissue-specific expression of the gene in skeletal muscle cells. Here, we report the
identification and characterization of a Kruppel-like zinc finger
protein, termed enolase repressor factor 1, that binds in a
sequence-specific manner to the G-rich box and functions as a repressor
of the enolase gene transcription in transient transfection assays.
Using fusion polypeptides of enolase repressor factor 1 and the
yeast GAL4 DNA-binding domain, we have identified an amino-terminal
region responsible for the transcriptional repression activity, whereas
a carboxyl-terminal region was shown to contain a potential
transcriptional activation domain. The expression of this protein
decreases in developing skeletal muscles, correlating with lack of
binding activity in nuclear extract from adult skeletal tissue, in
which novel binding activities have been detected. These results
suggest that in addition to the identified factor, which functionally
acts as a negative regulator and is enriched in embryonic muscle, the
G-rich box binds other factors, presumably exerting a positive control
on transcription. The interplay between factors that repress or
activate transcription may constitute a developmentally regulated
mechanism that modulates enolase gene expression in skeletal
muscle.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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