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(Received for publication, February 5, 1996, and in revised form, June 20, 1996)
From the Heinrich-Pette-Institut für experimentelle Virologie
und Immunologie an der Universität Hamburg,
20251 Hamburg, Germany
Expression of the nuclear domain-associated
proteins Sp100, PML, and NDP52, is enhanced by interferons (IFNs) on
the mRNA and protein level. Increase both of Sp100 and PML mRNA
is due to enhanced transcription of the corresponding genes which
occurs independently of cellular protein synthesis immediately upon
IFN-
Volume 271, Number 41,
Issue of October 11, 1996
pp. 25253-25260
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
Activation Site and an Imperfect IFN-stimulated
Response Element Which Mediate Type I IFN Inducibility
addition. Here, we describe the molecular cloning and
functional analysis of the Sp100 promoter. DNA sequence
analysis revealed potential binding sites for several constitutive and
IFN-inducible transcription factors. Consistent with the absence of a
TATA box and an initiator element, several transcription initiation
sites were found. Transient expression studies identified an imperfect
IFN-stimulated response element within the first 100 nucleotides
upstream of the major transcription start site. This element rendered a
heterologous promoter IFN--inducible and bound IFN-stimulated gene
factor 2 strongly but IFN-stimulated gene factor 3 only weakly. An
IFN-
activation site approximately 500 base pairs upstream of the
IFN-stimulated response element was found to bind three IFN-
/
activation factors upon IFN- induction and conferred both type I and
type II IFN inducibility upon a heterologous promoter. These data
demonstrate a novel arrangement of a nonoverlapping IFN- activation
site and an IFN-stimulated response element mediating type I IFN
inducibility, previously not reported for other IFN-stimulable
promoters.
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