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(Received for publication, June 13, 1996)
From the Departments of Kinesiology and Biology, Faculty of Pure
and Applied Science, York University, Toronto, Ontario M3J 1P3,
Canada
Tissue-specific gene expression can be mediated
by complex transcriptional regulatory mechanisms. Based on the
dichotomy of the ubiquitous distribution of the myocyte enhancer factor
2 (MEF2) gene mRNAs compared to their cell
type-restricted activity, we investigated the basis for their tissue
specificity. Electrophoretic mobility shift assays using the muscle
creatine kinase MEF2 DNA binding site as a probe showed that HeLa,
Schneider, L6E9 muscle, and C2C12 muscle cells have a functional MEF2
binding activity that is indistinguishable based on competition
analysis. Interestingly, chloramphenicol acetyltransferase reporter
assays showed MEF2 site-dependent
trans-activation in myogenic C2C12 cells but no
trans-activation by the endogenous MEF2 proteins in HeLa
cells. By immunofluorescence, we detected abundant nuclear localized
MEF2A and MEF2D protein expression in HeLa cells and C2C12 muscle
cells. Using immuno-gel shift analysis and also co-immunoprecipitation
studies, we show that the predominant MEF2 DNA binding complex bound to
MEF2 sites from either the muscle creatine kinase or c-jun
regulatory regions in C2C12 muscle cells is comprised of a MEF2A
homodimer, whereas in HeLa cells, it is a MEF2A:MEF2D heterodimer.
Thus, the presence of MEF2 DNA binding complexes is not necessarily
coupled with trans-activation of target genes. The ability
of the MEF2 proteins to activate transcription in vivo
correlates with the specific dimer composition of the DNA binding
complex and the cellular context.
Volume 271, Number 40,
Issue of October 4, 1996
pp. 24927-24933
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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