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Vol. 13, No. 14, pp. 1807-1821, July 15, 1999
Howard Hughes Medical Institute and Cold Spring Harbor Laboratory,
Cold Spring Harbor, New York 11724 USA
snRNA gene transcription is activated in part by recruitment of
SNAPc to the core promoter through protein-protein contacts with the POU domain of the enhancer-binding factor Oct-1. We show that
a mini-SNAPc consisting of a subset of SNAPc
subunits is capable of directing both RNA polymerase II (Pol II) and
Pol III snRNA gene transcription. Mini-SNAPc cannot be
recruited by Oct-1, but binds as efficiently to the promoter as
SNAPc together with Oct-1 and directs activated RNA Pol III
transcription. Thus, SNAPc represses its own binding to DNA,
and repression is relieved by interactions with the Oct-1 POU domain
that promote cooperative binding. We have shown previously that TBP
also represses its own binding, and in that case repression is relieved
by cooperative interactions with SNAPc. This may represent a
general mechanism to ensure that core promoter-binding factors, which
have strikingly slow off-rates, are recruited specifically to promoter
sequences rather than to cryptic-binding sites in the genome.
[Key Words: snRNA genes; SNAPc; PSE; Oct-1 POU; TBP; mini-SNAPc; transcription activation]
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