PMID- 9280343
OWN - NLM
STAT- MEDLINE
DCOM- 19971002
LR  - 20191210
IS  - 1356-9597 (Print)
IS  - 1356-9597 (Linking)
VI  - 2
IP  - 5
DP  - 1997 May
TI  - Identification of an extended half-site motif required for the function of 
      peroxisome proliferator-activated receptor alpha.
PG  - 315-27
AB  - BACKGROUND: Peroxisome proliferator-activated receptors (PPARs) belong to the 
      nuclear hormone receptor superfamily and regulate many genes of the proteins 
      involved in lipid metabolism, including peroxisomal acyl-CoA oxidase (AOX). 
      Through heterodimerization with retinoid X receptors (RXRs), PPAR was believed to 
      recognize the sequence elements consisting of two directly repeating 6-bp 
      half-sites spaced by one nucleotide (DR-1), located in the regulatory regions of 
      these genes. RESULTS: Employing the peroxisome proliferator-responsive enhancer 
      of the rat AOX gene, we analysed the minimal sequence requirements for enhancer 
      activity and PPARalpha/RXRalpha binding. We found that the sequence just 
      downstream of the DR-1 motif is indispensable for both functions. By a direct 
      selection procedure of high-affinity binding sites from a random sequence pool, 
      we identified a consensus sequence at the four positions next to DR-1. We also 
      suggest that PPARalpha binds to the downstream half-site, whereas RXRalpha binds 
      to the upstream half-site of the AOX DR-1. CONCLUSIONS: An extended half-site of 
      10-bp, but not a simple 6-bp half-site, is required for the PPARalpha binding, 
      upon heterodimer formation with RXRalpha. The binding polarity of 
      PPARalpha/RXRalpha seems to be opposite to that of other RXR-involving 
      heterodimers.
FAU - Osada, S
AU  - Osada S
AD  - Department of Life Science, Himeji Institute of Technology, Kamigori, Hyogo, 
      Japan.
FAU - Tsukamoto, T
AU  - Tsukamoto T
FAU - Takiguchi, M
AU  - Takiguchi M
FAU - Mori, M
AU  - Mori M
FAU - Osumi, T
AU  - Osumi T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Genes Cells
JT  - Genes to cells : devoted to molecular & cellular mechanisms
JID - 9607379
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Receptors, Cytoplasmic and Nuclear)
RN  - 0 (Receptors, Retinoic Acid)
RN  - 0 (Retinoid X Receptors)
RN  - 0 (Transcription Factors)
RN  - EC 1.- (Oxidoreductases)
RN  - EC 1.13.12.- (Luciferases)
RN  - EC 1.3.3.- (peroxisomal acyl-CoA oxidase)
RN  - EC 1.3.3.6 (Acyl-CoA Oxidase)
SB  - IM
MH  - Acyl-CoA Oxidase
MH  - Animals
MH  - Binding Sites/genetics
MH  - Cell Line
MH  - Consensus Sequence/genetics
MH  - DNA-Binding Proteins/*metabolism
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Enhancer Elements, Genetic/genetics
MH  - Genes, Reporter/genetics
MH  - Luciferases/metabolism
MH  - Nuclear Proteins/*metabolism
MH  - Oxidoreductases/*genetics
MH  - Plasmids/genetics
MH  - Point Mutation
MH  - Rats
MH  - Receptors, Cytoplasmic and Nuclear/*metabolism
MH  - Receptors, Retinoic Acid/*metabolism
MH  - Retinoid X Receptors
MH  - Sequence Alignment
MH  - Sequence Deletion
MH  - Transcription Factors/*metabolism
MH  - Transfection
EDAT- 1997/05/01 00:00
MHDA- 1997/05/01 00:01
CRDT- 1997/05/01 00:00
PHST- 1997/05/01 00:00 [pubmed]
PHST- 1997/05/01 00:01 [medline]
PHST- 1997/05/01 00:00 [entrez]
AID - 10.1046/j.1365-2443.1997.1220319.x [doi]
PST - ppublish
SO  - Genes Cells. 1997 May;2(5):315-27. doi: 10.1046/j.1365-2443.1997.1220319.x.