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J Biol Chem, Vol. 274, Issue 51, 36649-36655, December 17, 1999
From the DNA methylation inhibits transcription driven by
the collagen
A Methylation-responsive MDBP/RFX Site Is in the First Exon
of the Collagen
2(I) Promoter*
,§
Department of Biochemistry, Boston
University School of Medicine, Boston, Massachusetts 02118, the
§ Boston Department of Veterans Affairs Medical Center,
Boston, Massachusetts 02118, and the ¶ Human Genetics Program
and Department of Biochemistry, Tulane Medical School,
New Orleans, Louisiana 70112
2(I) promoter and the 5' end of the gene in transient
transfection and in vitro transcription assays. DNA-binding
proteins in a unique family of ubiquitously expressed proteins,
methylated DNA-binding protein (MDBP)/regulatory factor for X box
(RFX), form specific complexes with a sequence overlapping the
transcription start site of the collagen 2(I) gene. Complex
formation increased when the CpG site at +7 base pairs from the
transcription start site was methylated. The identity of the protein
was demonstrated by co-migration and cross-competition for a
characteristic slowly migrating doublet complex formed on MDBP/RFX
recognition sequences and the collagen sequences by band shift assays.
A RFX1-specific antibody supershifted the collagen DNA-protein
complexes. Furthermore, in vitro translated RFX1 protein
formed a specific complex with the collagen sequence that was also
supershifted with the RFX1 antibody. MDBP/RFX displayed a higher
affinity binding to the collagen sequence if the CpG at +7 was mutated
in a manner similar to TpG. This same mutation within reporter
constructs inhibited transcription in transfection and in
vitro transcription assay. These results support the hypothesis
that DNA methylation-induced inactivation of collagen 2(I) gene
transcription is mediated, in part, by increased binding of MDBP/RFX to
the first exon in response to methylation in this region.
*
This work was supported in part by National Institutes of
Health Grants R01-CA23540 and P50-HL56386 and by the Department of
Veterans Affairs merit review program.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.
To whom correspondence should be addressed: Dept. of
Biochemistry, Boston University School of Medicine, 715 Albany St.,
Boston, MA 02118. Tel.: 617-638-4159; Fax: 617-638-5339; E-mail:
smith@biochem.bumc.bu.edu.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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