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(Received for publication, April 16, 1997, and in revised form, May 23, 1997)
From the Institut de Biologie Animale, Université de
Lausanne, Bâtiment de Biologie, CH-1015
Lausanne, Switzerland
The malic enzyme (ME) gene is a target for both
thyroid hormone receptors and peroxisome proliferator-activated
receptors (PPAR). Within the ME promoter, two direct repeat (DR)-1-like elements, MEp and MEd, have been identified as putative PPAR response elements (PPRE). We demonstrate that only MEp and not MEd is able to
bind PPAR/retinoid X receptor (RXR) heterodimers and mediate peroxisome
proliferator signaling. Taking advantage of the close sequence
resemblance of MEp and MEd, we have identified crucial determinants of
a PPRE. Using reciprocal mutation analyses of these two elements, we
show the preference for adenine as the spacing nucleotide between the
two half-sites of the PPRE and demonstrate the importance of the two
first bases flanking the core DR1 in 5
Volume 272, Number 32,
Issue of August 8, 1997
pp. 20108-20117
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
A FUNCTIONAL ANALYSIS OF THE MALIC ENZYME GENE PPAR
RESPONSE ELEMENT
. This latter feature of the
PPRE lead us to consider the polarity of the PPAR/RXR heterodimer bound
to its cognate element. We demonstrate that, in contrast to the
polarity of RXR/TR and RXR/RAR bound to DR4 and DR5 elements
respectively, PPAR binds to the 5 extended half-site of the response
element, while RXR occupies the 3 half-site. Consistent with this
polarity is our finding that formation and binding of the PPAR/RXR
heterodimer requires an intact hinge T region in RXR while its
integrity is not required for binding of the RXR/TR heterodimer to a
DR4.
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