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J Biol Chem, Vol. 273, Issue 37, 24239-24248, September 11, 1998
From the Institut de Biologie Animale, Université de
Lausanne, Bâtiment de Biologie,
CH-1015 Lausanne, Switzerland
While there is evidence that the two ubiquitously
expressed thyroid hormone (T3) receptors, TR
Transcriptional Regulatory Patterns of the Myelin Basic Protein
and Malic Enzyme Genes by the Thyroid Hormone Receptors
1 and
1
1 and TR
1, have
distinct functional specificities, the mechanism by which they
discriminate potential target genes remains largely unexplained. In
this study, we demonstrate that the thyroid hormone response elements
(TRE) from the malic enzyme and myelin basic protein genes
(METRE and MBPTRE) respectively, are not
functionally equivalent. The METRE, which is a direct repeat motif with a 4-base pair gap between the two half-site hexamers
binds thyroid hormone receptor as a heterodimer with 9-cis-retinoic acid receptor (RXR) and mediates a high
T3-dependent activation in response to TR1 or TR1 in
NIH3T3 cells. In contrast, the MBPTRE, which consists of an
inverted palindrome formed by two hexamers spaced by 6 base pairs,
confers an efficient transactivation by TR1 but a poor
transactivation by TR1. While both receptors form heterodimers with
RXR on MBPTRE, the poor transactivation by TR1
correlates also with its ability to bind efficiently as a monomer. This
monomer, which is only observed with TR1 bound to
MBPTRE, interacts neither with N-CoR nor with SRC-1,
explaining its functional inefficacy. However, in Xenopus
oocytes, in which RXR proteins are not detectable, the transactivation
mediated by TR1 and TR1 is equivalent and independent of a RXR
supply, raising the question of the identity of the thyroid hormone
receptor partner in these cells. Thus, in mammalian cells, the binding characteristics of TR1 to MBPTRE (i.e. high
monomer binding efficiency and low transactivation activity) might
explain the particular pattern of T3 responsiveness of MBP gene
expression during central nervous system development.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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