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J Biol Chem, Vol. 273, Issue 43, 27988-27997, October 23, 1998
From the Department of Molecular and Experimental Medicine, The
Scripps Research Institute, La Jolla, California 92037
Heterodimers of the peroxisome
proliferator-activated receptors (PPAR) and the retinoid X receptors
(RXR) recognize response elements (PPREs) that exhibit the
consensus sequence
5'-A(A/T)CT(A/G)GGNCAAAG(G/T)TCA-3'. The
consensus PPRE includes both a 5'-extension and a direct repeat (DR1)
comprised of two canonical core recognition sequences
(underlined) for nuclear receptor zinc fingers separated by
a single nucleotide spacer. The extended binding site recognized by
PPARs is very similar to sites that bind monomers of the nuclear
receptors Rev-ErbA and ROR suggesting that the latter could bind to
PPREs and affect gene transcription. However, Rev-ErbA and ROR bind
weakly to naturally occurring PPREs relative to the consensus binding
site, and significant effects on PPAR
A Carboxyl-terminal Extension of the Zinc Finger Domain
Contributes to the Specificity and Polarity of Peroxisome
Proliferator-activated Receptor DNA Binding
transactivation of a CYP4A6-Z
reporter were not observed. In contrast, PPAR/RXR heterodimers bind to
a DR2 element containing the conserved 5'-extended sequence that is
recognized by dimers of ROR or Rev-ErbA. PPAR/RXR positively
regulate transcription from this element, and co-expression of Rev-ErbA blocks this effect. The nuclear receptors NGFI-B and ROR utilize a
carboxyl-terminal extension (CTE) of the zinc finger DNA binding domain
in their interactions with the 5'-extension of a single zinc
finger-binding site. DNA binding domains (DBD) of PPARs , 
, and
that contain the zinc finger motif and a CTE display binding to
core recognition sequences that is dependent on the 5'-extended
sequence found in PPREs. Unlike DBDs of other nuclear receptors that
form heterodimers with RXR, the PPAR-DBDs did not exhibit cooperative
binding with the DBD of RXR and exhibit the opposite polarity for
binding to the direct repeat motif. In contrast to the corresponding
DBD of RXR, the PPAR-DBDs bind as monomers to a single extended binding
site as well as to the consensus PPRE. A chimera linking the zinc
finger domain of RXR to the CTE from PPAR bound to a single
extended binding site indicating a functional role for the CTE of PPARs
in extended binding site recognition.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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