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J Biol Chem, Vol. 275, Issue 19, 14190-14197, May 12, 2000
From the Department of Surgery, Endocrine Unit, Uppsala University
Hospital, S-751 85 Uppsala, Sweden, the Megalin/low density lipoprotein receptor-related
protein 2 (LRP-2) is an endocytic receptor expressed in highly
specialized cell types such as parathyroid cells and epithelia of the
kidney. Previous experiments identified a nonconsensus TATA element,
with the sequence TAGAAAA, as crucial for accurate and efficient
transcription from the LRP-2 promoter. Here we show that, in addition
to the TAGA element, promoter sequences downstream of the transcription start site contribute significantly to transcription both in
vitro and in transfected cells. Deletion and point mutational
analyses reveal that the promoter region located between positions +5
and +11 (sequence TTTTGGC) is of particular importance. Complementation experiments in nuclear extracts lacking transcription factor IID (TFIID) activity show that TATA-binding protein-associated factors of
TFIID are essential for the function of LRP-2 downstream promoter sequences. Interestingly, DNase I footprinting studies show that the
downstream region between positions +5 and +11 does not significantly affect overall TFIID affinity to the promoter but that it profoundly affects the topology of the TFIID·promoter complex not only
downstream of the transcription start site, but in particular in the
TATA box region. Our observations suggest a model for a novel
downstream sequence function, in which TATA-binding protein-associated
factor-promoter interactions downstream of the transcription start site
modulate TFIID-DNA interactions in the TATA box region.
Downstream Promoter Sequences Facilitate the Formation of a
Specific Transcription Factor IID-Promoter Complex Topology Required
for Efficient Transcription from the Megalin/Low Density
Lipoprotein Receptor-related Protein 2 Promoter*
,, Eukaryotic
Gene Regulation Laboratory, Marie Curie Research Institute, The Chart,
Oxted, Surrey RH8 0TL, United Kingdom, and the
§ Laboratory of Biochemistry and Molecular Biology, The
Rockefeller University, New York, New York 10021
*
This work was supported by grants from the Swedish Medical
Research Council, Uppsala University, and the Marie Curie Research Institute (to G. W., A. K., and T. O., respectively).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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