Nucleic Acids Research, Vol 26, Issue 7 1793-1800, Copyright © 1998 by Oxford University Press
EL Kim, H Peng, FM Esparza, SZ Maltchenko and MK Stachowiak
Tyrosine hydroxylase (TH) is expressed specifically in catecholaminergic
cells. We have identified a novel regulatory sequence in the upstream
region of the bovine TH gene promoter formed by a dyad symmetry element
(DSE1;-352/-307 bp). DSE1 supports TH promoter activity in TH-expressing
bovine adrenal medulla chromaffin (BAMC) cells and inhibits promoter
activity in non-expressing TE671 cells. DNase I footprinting of relaxed TH
promoter DNA showed weak binding of nuclear BAMC cell proteins to a short
sequence in the right DSE1 arm. In BAMC cells, deletion of the right arm
markedly reduced the expression of luciferase from the TH promoter.
However, deletion of the left DSE1 arm or its reversed orientation (RevL)
also inactivated the TH promoter. In supercoiled TH promoter, DSE1 assumes
a cruciform-like conformation i.e., it binds cruciform-specific 2D3
antibody, and S1 nuclease-cleavage and OsO4-modification assays have
identified an imperfect cruciform extruded by the DSE1. DNase I
footprinting of supercoiled plasmid showed that cruciformed DSE1 is
targeted by nuclear proteins more efficiently than the linear duplex isomer
and that the protected site encompasses the left arm and center of DSE1.
Our results suggest that the disruption of intrastrand base-pairing
preventing cruciform formation and protein binding to DSE1 is responsible
for its inactivation in DSE1 mutants. DSE1 cruciform may act as a target
site for activator (BAMC cells) and repressor (TE671) proteins. Its
extrusion emerges as a novel mechanism that controls cell-specific promoter
activity.
ARTICLES
Cruciform-extruding regulatory element controls cell-specific activity of the tyrosine hydroxylase gene promoter
Laboratory of Molecular Neurobiology, Division of Neurobiology, Barrow Neurological Institute, Phoenix, AZ 85013, USA.
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