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J Biol Chem, Vol. 275, Issue 1, 530-538, January 7, 2000
From the Drosophila Runt is the founding
member of a family of related transcription factors involved in the
regulation of a variety of cell-differentiation events in invertebrates
and vertebrates. Runt-related proteins act as both transactivators and
transcriptional repressors, suggesting that
context-dependent mechanisms modulate their transcriptional
properties. The aim of this study was to elucidate the molecular
mechanisms that contribute to the regulation of the functions of the
mammalian Runt-related protein, Cbfa1. Here we provide the first
demonstration that Cbfa1 (as well as the related protein, Cbfa2/AML1)
physically interacts with the basic helix loop helix transcription
factor, HES-1, a mammalian counterpart of the Drosophila
Hairy and Enhancer of split proteins. This interaction is mediated by
the carboxyl-terminal domains of Cbfa1 and HES-1, but does not require
their respective tetrapeptide motifs, WRPY and WRPW. Our studies also
show that HES-1 can antagonize the binding of Cbfa1 to mammalian
transcriptional corepressors of the Groucho family. Moreover, HES-1 can
potentiate Cbfa1-mediated transactivation in transfected cells. Taken
together, these findings implicate HES-1 in the transcriptional
functions of Cbfa1 and suggest that the concerted activities of Groucho
and HES proteins modulate the functions of mammalian Runt-related proteins.
The Mammalian Basic Helix Loop Helix Protein HES-1 Binds to and
Modulates the Transactivating Function of the Runt-related Factor
Cbfa1*
,,,
Center for Neuronal Survival, Montreal
Neurological Institute, McGill University, Montreal, Quebec, H3A 2B4
Canada and the § Department of Human and Molecular Genetics,
Baylor College of Medicine, Houston, Texas 77030
*
This work was supported by National Institutes of Health
Grants DE11290 and HD97006 and a Basic Science Award of the March of
Dimes Foundation (to G. K.) and Medical Research Council of Canada
Grants MT-13957 and GR-14971 (to S. S.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Scholar of the Fonds de la Recherche en Sante du Quebec and
Killam Scholar of the Montreal Neurological Institute. To whom correspondence should be addressed: Tel.: 514-398-3946; Fax:
514-398-1319; E-mail: mdst@musica.mcgill.ca.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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